{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,16]],"date-time":"2026-09-16T16:45:45Z","timestamp":1789577145230,"version":"build-2803163510"},"reference-count":234,"publisher":"MDPI AG","issue":"10","license":[{"start":{"date-parts":[[2019,9,25]],"date-time":"2019-09-25T00:00:00Z","timestamp":1569369600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100003593","name":"Conselho Nacional de Desenvolvimento Cient\u00edfico e Tecnol\u00f3gico","doi-asserted-by":"publisher","award":["407625\/2013-5"],"award-info":[{"award-number":["407625\/2013-5"]}],"id":[{"id":"10.13039\/501100003593","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Toxins"],"abstract":"<jats:p>Arthropoda is a phylum of invertebrates that has undergone remarkable evolutionary radiation, with a wide range of venomous animals. Arthropod venom is a complex mixture of molecules and a source of new compounds, including antimicrobial peptides (AMPs). Most AMPs affect membrane integrity and produce lethal pores in microorganisms, including protozoan pathogens, whereas others act on internal targets or by modulation of the host immune system. Protozoan parasites cause some serious life-threatening diseases among millions of people worldwide, mostly affecting the poorest in developing tropical regions. Humans can be infected with protozoan parasites belonging to the genera Trypanosoma, Leishmania, Plasmodium, and Toxoplasma, responsible for Chagas disease, human African trypanosomiasis, leishmaniasis, malaria, and toxoplasmosis. There is not yet any cure or vaccine for these illnesses, and the current antiprotozoal chemotherapeutic compounds are inefficient and toxic and have been in clinical use for decades, which increases drug resistance. In this review, we will present an overview of AMPs, the diverse modes of action of AMPs on protozoan targets, and the prospection of novel AMPs isolated from venomous arthropods with the potential to become novel clinical agents to treat protozoan-borne diseases.<\/jats:p>","DOI":"10.3390\/toxins11100563","type":"journal-article","created":{"date-parts":[[2019,9,26]],"date-time":"2019-09-26T03:06:51Z","timestamp":1569467211000},"page":"563","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":42,"title":["Natural Occurrence in Venomous Arthropods of Antimicrobial Peptides Active against Protozoan Parasites"],"prefix":"10.3390","volume":"11","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-6549-7826","authenticated-orcid":false,"given":"Elias Ferreira","family":"Sabi\u00e1 J\u00fanior","sequence":"first","affiliation":[{"name":"Departamento de Ci\u00eancias Fisiol\u00f3gicas, Instituto de Ci\u00eancias Biol\u00f3gicas, Universidade de Bras\u00edlia, Bras\u00edlia, DF 70910-900, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2264-5016","authenticated-orcid":false,"given":"Luis Felipe Santos","family":"Menezes","sequence":"additional","affiliation":[{"name":"Departamento de Ci\u00eancias Fisiol\u00f3gicas, Instituto de Ci\u00eancias Biol\u00f3gicas, Universidade de Bras\u00edlia, Bras\u00edlia, DF 70910-900, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0136-0062","authenticated-orcid":false,"given":"Israel Flor Silva","family":"de Ara\u00fajo","sequence":"additional","affiliation":[{"name":"Departamento de Ci\u00eancias Fisiol\u00f3gicas, Instituto de Ci\u00eancias Biol\u00f3gicas, Universidade de Bras\u00edlia, Bras\u00edlia, DF 70910-900, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Elisabeth Ferroni","family":"Schwartz","sequence":"additional","affiliation":[{"name":"Departamento de Ci\u00eancias Fisiol\u00f3gicas, Instituto de Ci\u00eancias Biol\u00f3gicas, Universidade de Bras\u00edlia, Bras\u00edlia, DF 70910-900, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2019,9,25]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"650","DOI":"10.1590\/0037-8682-0242-2015","article-title":"Venomous and poisonous arthropods: Identification, clinical manifestations of envenomation, and treatments used in human injuries","volume":"48","author":"Junior","year":"2015","journal-title":"Rev. Soc. Bras. Med. Trop."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1146\/annurev-ento-120710-100659","article-title":"Reevaluating the arthropod tree of life","volume":"57","author":"Giribet","year":"2012","journal-title":"Annu. Rev. \u00c8ntomol."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1002\/bip.22100","article-title":"Arthropod venoms: A vast arsenal of insecticidal neuropeptides","volume":"98","author":"Schwartz","year":"2012","journal-title":"Biopolymers"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1016\/j.toxicon.2018.07.018","article-title":"Structural diversity of arthropod venom toxins","volume":"152","author":"Daly","year":"2018","journal-title":"Toxicon"},{"key":"ref_5","first-page":"1","article-title":"Animal biodiversity: An outline of higher-level classification and survey of taxonomic richness (COVER)","volume":"3148","author":"Zhang","year":"2011","journal-title":"Zootaxa"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"7519","DOI":"10.1073\/pnas.1502408112","article-title":"New approaches narrow global species estimates for beetles, insects, and terrestrial arthropods","volume":"112","author":"Stork","year":"2015","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"1838","DOI":"10.1093\/molbev\/msx147","article-title":"Evolutionary History of Chemosensory-Related Gene Families across the Arthropoda","volume":"34","author":"Eyun","year":"2017","journal-title":"Mol. Boil. Evol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1146\/annurev.en.20.010175.001401","article-title":"Adaptations of Arthropoda to arid environments","volume":"20","year":"1975","journal-title":"Annu. Rev. \u00c8ntomol."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"367","DOI":"10.1111\/j.1469-185X.1989.tb00681.x","article-title":"Adaptations Of Terrestrial Arthropods To The Alpine Environment","volume":"64","year":"1989","journal-title":"Boil. Rev."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"1883","DOI":"10.1126\/science.1129844","article-title":"The origin of insects","volume":"314","author":"Glenner","year":"2006","journal-title":"Science"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"4611","DOI":"10.1038\/ncomms5611","article-title":"Compact genome of the Antarctic midge is likely an adaptation to an extreme environment","volume":"5","author":"Kelley","year":"2014","journal-title":"Nat. Commun."},{"key":"ref_12","unstructured":"Marcussi, S., Arantes, E.C., and Soares, A.M. (2011). Escorpi\u00f5es: Biologia, Envenenamento e Mecanismos de A\u00e7\u00e3o de Suas Toxinas, FUNPEC Editora. [1\u00aa edi\u00e7\u00e3o]."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"84","DOI":"10.1016\/j.toxicon.2018.11.433","article-title":"Arthropod venoms: Biochemistry, ecology and evolution","volume":"158","author":"Suranse","year":"2019","journal-title":"Toxicon"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1016\/j.toxicon.2018.09.004","article-title":"Entomo-venomics: The evolution, biology and biochemistry of insect venoms","volume":"154","author":"Walker","year":"2018","journal-title":"Toxicon"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1016\/j.tree.2012.10.020","article-title":"Complex cocktails: The evolutionary novelty of venoms","volume":"28","author":"Casewell","year":"2013","journal-title":"Trends Ecol. Evol."},{"key":"ref_16","doi-asserted-by":"crossref","unstructured":"Suranse, V., Srikanthan, A., and Sunagar, K. (2018). Animal Venoms: Origin, diversity and evolution. eLS, John Wiley & Sons, Ltd.","DOI":"10.1002\/9780470015902.a0000939.pub2"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1146\/annurev.en.27.010182.002011","article-title":"Biochemistry of Insect Venoms","volume":"27","author":"Schmidt","year":"1982","journal-title":"Annu. Rev. Entomol."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1146\/annurev.en.08.010163.000245","article-title":"Insect Toxins and Venoms","volume":"8","author":"Beard","year":"1963","journal-title":"Annu. Rev. Entomol."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/j.toxicon.2018.11.312","article-title":"Arthropod assassins: Crawling biochemists with diverse toxin pharmacopeias","volume":"158","author":"Herzig","year":"2019","journal-title":"Toxicon"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"3215","DOI":"10.1007\/s00018-018-2768-1","article-title":"Giant fish-killing water bug reveals ancient and dynamic venom evolution in Heteroptera","volume":"75","author":"Walker","year":"2018","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1016\/j.jprot.2014.10.014","article-title":"Peptidomics combined with cDNA library unravel the diversity of centipede venom","volume":"114","author":"Rong","year":"2015","journal-title":"J. Proteom."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"4832","DOI":"10.3390\/toxins7114832","article-title":"Centipede Venoms and Their Components: Resources for Potential Therapeutic Applications","volume":"7","author":"Hakim","year":"2015","journal-title":"Toxins"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1590\/1678-9199-jvatitd-1482-18","article-title":"Proteome of fraction from Tityus serrulatus venom reveals new enzymes and toxins","volume":"25","author":"Amorim","year":"2019","journal-title":"J. Venom. Anim. Toxins Incl. Trop. Dis."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"893","DOI":"10.1016\/S0300-9084(00)01166-4","article-title":"Structure and pharmacology of spider venom neurotoxins","volume":"82","author":"Escoubas","year":"2000","journal-title":"Biochimie"},{"key":"ref_25","first-page":"555","article-title":"Pharmacological characterization of venoms from three theraphosid spiders: Poecilotheria regalis, Ceratogyrus darlingi and Brachypelma epicureanum","volume":"21","year":"2015","journal-title":"J. Venom. Anim. Toxins Incl. Trop. Dis."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1093\/molbev\/mst199","article-title":"The first venomous crustacean revealed by transcriptomics and functional morphology: Remipede venom glands express a unique toxin cocktail dominated by enzymes and a neurotoxin","volume":"31","author":"Blanke","year":"2014","journal-title":"Mol. Biol. Evol."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1146\/annurev-ento-020117-043348","article-title":"How many species of insects and other terrestrial arthropods are there on Earth?","volume":"63","author":"Stork","year":"2018","journal-title":"Annu. Rev. Entomol."},{"key":"ref_28","unstructured":"Bonato, L., Chagas, A., Edgecombe, G.D., Lewis, J.G.E., Minelli, A., Pereira, L.A., Shelley, R.M., Stoev, P., and Zapparoli, M. (2019, July 12). ChiloBase 2.0\u2014A World Catalogue of Centipedes (Chilopoda). Available online: http:\/\/chilobase.biologia.unipd.it\/."},{"key":"ref_29","unstructured":"Rein, J.O. (2019, July 12). The Scorpion Files. Available online: https:\/\/www.ntnu.no\/ub\/scorpion-files\/."},{"key":"ref_30","unstructured":"(2019, July 12). Natural History Museum Bern World Spider Catalog. Version 20.0. Available online: https:\/\/wsc.nmbe.ch\/."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1186\/1742-9994-11-47","article-title":"Are ticks venomous animals?","volume":"11","year":"2014","journal-title":"Front. Zool."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"624","DOI":"10.1177\/0091270003253349","article-title":"Pharmacokinetics and Pharmacodynamics of Intrathecal Ziconotide in Chronic Pain Patients","volume":"43","author":"Wermeling","year":"2003","journal-title":"J. Clin. Pharmacol."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1038\/225379a0","article-title":"Activity of various fractions of bradykinin potentiating factor against angiotensin I converting enzyme","volume":"225","author":"Ferreira","year":"1970","journal-title":"Nature"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"464","DOI":"10.1016\/j.toxicon.2010.12.016","article-title":"The development of Byetta (exenatide) from the venom of the Gila monster as an anti-diabetic agent","volume":"59","author":"Furman","year":"2012","journal-title":"Toxicon"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1016\/S0952-7915(02)00005-5","article-title":"Drosophila immunity: Paths and patterns","volume":"15","author":"Hultmark","year":"2003","journal-title":"Curr. Opin. Immunol."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1016\/S0167-7799(00)88947-7","article-title":"Amphibian skin: A promising resource for antimicrobial peptides","volume":"13","author":"Barra","year":"1995","journal-title":"Trends Biotechnol."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"536","DOI":"10.1016\/j.ijantimicag.2004.09.005","article-title":"Antimicrobial peptides: Premises and promises","volume":"24","author":"Reddy","year":"2004","journal-title":"Int. J. Antimicrob. Agents"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"465","DOI":"10.1016\/S0924-8579(03)00180-8","article-title":"Antimicrobial peptides in animals and their role in host defences","volume":"22","author":"Brogden","year":"2003","journal-title":"Int. J. Antimicrob. Agents"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1016\/j.coi.2005.11.004","article-title":"Cationic host defense (antimicrobial) peptides","volume":"18","author":"Brown","year":"2006","journal-title":"Curr. Opin. Immunol."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"2449","DOI":"10.2174\/092986706777935041","article-title":"Peptides and peptidomimetics in medicine, surgery and biotechnology","volume":"13","author":"Gentilucci","year":"2006","journal-title":"Curr. Med. Chem."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"313","DOI":"10.1128\/AAC.36.2.313","article-title":"Augmentation of the antibacterial activity of magainin by positive-charge chain extension","volume":"36","author":"Bessalle","year":"1992","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"2998","DOI":"10.1016\/j.bbamem.2015.09.012","article-title":"The efficacy of trivalent cyclic hexapeptides to induce lipid clustering in PG\/PE membranes correlates with their antimicrobial activity","volume":"1848","author":"Finger","year":"2015","journal-title":"Biochim. Biophys. Acta-Biomembr."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"723","DOI":"10.1128\/iai.31.2.723-731.1981","article-title":"Microbicidal cationic proteins of rabbit alveolar macrophages: Amino acid composition and functional attributes","volume":"31","author":"Szklarek","year":"1981","journal-title":"Infect. Immun."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"975","DOI":"10.1038\/nature04051","article-title":"Plectasin is a peptide antibiotic with therapeutic potential from a saprophytic fungus","volume":"437","author":"Mygind","year":"2005","journal-title":"Nature"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"3967","DOI":"10.1128\/AAC.00542-08","article-title":"Mucroporin, the first cationic host defense peptide from the venom of Lychas mucronatus","volume":"52","author":"Dai","year":"2008","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"3472","DOI":"10.1128\/AAC.01436-08","article-title":"Imcroporin, a new cationic antimicrobial peptide from the venom of the scorpion Isometrus maculates","volume":"53","author":"Zhao","year":"2009","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"2245","DOI":"10.2174\/0929867324666171106155936","article-title":"Antimicrobial peptides of marine crustaceans: The potential and challenges of developing therapeutic agents","volume":"25","author":"Zanjani","year":"2018","journal-title":"Curr. Med. Chem."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"389","DOI":"10.1016\/j.peptides.2012.09.012","article-title":"A novel class of antimicrobial peptides from the scorpion Heterometrus spinifer","volume":"38","author":"Nie","year":"2012","journal-title":"Peptides"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1016\/j.toxicon.2014.06.006","article-title":"Antimicrobial peptides from scorpion venoms","volume":"88","author":"Harrison","year":"2014","journal-title":"Toxicon"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"84","DOI":"10.1016\/j.toxicon.2010.10.008","article-title":"Vejovine, a new antibiotic from the scorpion venom of Vaejovis mexicanus","volume":"57","author":"Balderas","year":"2011","journal-title":"Toxicon"},{"key":"ref_51","doi-asserted-by":"crossref","unstructured":"Zhao, X., Wu, H., L\u00fc, H., Li, G., and Huang, Q. (2013). LAMP: A Database Linking Antimicrobial Peptides. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0066557"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1080\/08927014.2015.1021340","article-title":"BaAMPs: The database of biofilm-active antimicrobial peptides","volume":"31","author":"Maccari","year":"2015","journal-title":"Biofouling"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"24482","DOI":"10.1038\/srep24482","article-title":"DRAMP: A comprehensive data repository of antimicrobial peptides","volume":"6","author":"Fan","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"D1087","DOI":"10.1093\/nar\/gkv1278","article-title":"APD3: The antimicrobial peptide database as a tool for research and education","volume":"44","author":"Wang","year":"2016","journal-title":"Nucleic Acids Res."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"754","DOI":"10.1007\/s11837-015-1350-7","article-title":"Chimeric peptides as implant functionalization agents for titanium alloy implants with antimicrobial properties","volume":"67","author":"Yucesoy","year":"2015","journal-title":"JOM"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"1640005","DOI":"10.1142\/S2251237316400050","article-title":"Controlling the Biomimetic Implant Interface: Modulating Antimicrobial Activity by Spacer Design","volume":"4","author":"Wisdom","year":"2016","journal-title":"J. Mol. Eng. Mater."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"128","DOI":"10.1007\/s12275-018-7444-5","article-title":"The antimicrobial potential of a new derivative of cathelicidin from Bungarus fasciatus against methicillin-resistant Staphylococcus aureus","volume":"56","author":"Tajbakhsh","year":"2018","journal-title":"J. Microbiol."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"1236","DOI":"10.1016\/j.biochi.2010.02.023","article-title":"Structural determinants of host defense peptides for antimicrobial activity and target cell selectivity","volume":"92","author":"Takahashi","year":"2010","journal-title":"Biochimie"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1007\/s13238-010-0004-3","article-title":"Alpha-helical cationic antimicrobial peptides: Relationships of structure and function","volume":"1","author":"Huang","year":"2010","journal-title":"Protein Cell"},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1016\/S0014-5793(97)01310-0","article-title":"Structural organization of the bovine cathelicidin gene family and identification of a novel member 1","volume":"417","author":"Scocchi","year":"1997","journal-title":"FEBS Lett."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"15392","DOI":"10.3390\/molecules200815392","article-title":"The Potential Use of natural and structural analogues of antimicrobial peptides in the fight against neglected tropical diseases","volume":"20","author":"Lewies","year":"2015","journal-title":"Molecules"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1016\/j.jcis.2018.10.103","article-title":"Membrane targeting cationic antimicrobial peptides","volume":"537","author":"Ciumac","year":"2019","journal-title":"J. Colloid Interface Sci."},{"key":"ref_63","doi-asserted-by":"crossref","unstructured":"Kumar, P., Kizhakkedathu, J.N., and Straus, S.K. (2018). Antimicrobial peptides: diversity, mechanism of action and strategies to improve the activity and biocompatibility in vivo. Biomolecules, 8.","DOI":"10.3390\/biom8010004"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"1285","DOI":"10.1016\/j.bbamem.2006.03.016","article-title":"Peptide\u2013lipid interactions of the \u03b2-hairpin antimicrobial peptide tachyplesin and its linear derivatives from solid-state NMR","volume":"1758","author":"Doherty","year":"2006","journal-title":"Biochim. Biophys. Acta-Biomembr."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"879","DOI":"10.1016\/j.bbrc.2003.08.095","article-title":"Indolicidin, a 13-residue basic antimicrobial peptide rich in tryptophan and proline, interacts with Ca2+-calmodulin","volume":"309","author":"Sitaram","year":"2003","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"6014","DOI":"10.1073\/pnas.93.12.6014","article-title":"PR-39, a proline-rich antibacterial peptide that inhibits phagocyte NADPH oxidase activity by binding to Src homology 3 domains of p47 phox","volume":"93","author":"Shi","year":"1996","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"3124","DOI":"10.1096\/fj.14-266825","article-title":"Histatin-1, a histidine-rich peptide in human saliva, promotes cell-substrate and cell-cell adhesion","volume":"29","author":"Nazmi","year":"2015","journal-title":"FASEB J."},{"key":"ref_68","doi-asserted-by":"crossref","unstructured":"Stepensky, D. (2018). Pharmacokinetics of Toxin-Derived Peptide Drugs. Toxins, 10.","DOI":"10.3390\/toxins10110483"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1038\/nrd3591","article-title":"Designing antimicrobial peptides: Form follows function","volume":"11","author":"Fjell","year":"2012","journal-title":"Nat. Rev. Drug Discov."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"1047","DOI":"10.2217\/fmb.12.85","article-title":"Modes of action of Leishmanicidal antimicrobial peptides","volume":"7","author":"Marr","year":"2012","journal-title":"Future Microbiol."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"27501","DOI":"10.1074\/jbc.R110.128181","article-title":"Daptomycin, a bacterial lipopeptide synthesized by a nonribosomal machinery","volume":"285","author":"Robbel","year":"2010","journal-title":"J. Boil. Chem."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"4494","DOI":"10.1128\/JB.00011-12","article-title":"Daptomycin-mediated reorganization of membrane architecture causes mislocalization of essential cell division proteins","volume":"194","author":"Pogliano","year":"2012","journal-title":"J. Bacteriol."},{"key":"ref_73","first-page":"873","article-title":"Cockroaches, locusts, and envenomating arthropods: A promising source of antimicrobials","volume":"21","author":"Mosaheb","year":"2018","journal-title":"Iran. J. Basic Med. Sci."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"2142","DOI":"10.1016\/S0006-3495(99)77369-8","article-title":"A microscopic interaction model of maximum solubility of cholesterol in lipid bilayers","volume":"76","author":"Huang","year":"1999","journal-title":"Biophys. J."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"12629","DOI":"10.1021\/bi060610x","article-title":"Ceramide drives cholesterol out of the ordered lipid bilayer phase into the crystal phase in 1-Palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine\/cholesterol\/ceramide ternary mixtures","volume":"45","author":"Ali","year":"2006","journal-title":"Biochemistry"},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S0005-2736(99)00197-2","article-title":"Why and how are peptide\u2013lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes","volume":"1462","author":"Matsuzaki","year":"1999","journal-title":"Biochim. Biophys. Acta-Biomembr."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"1681","DOI":"10.1016\/j.peptides.2003.08.023","article-title":"The relationship between peptide structure and antibacterial activity","volume":"24","author":"Powers","year":"2003","journal-title":"Peptides"},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"406","DOI":"10.1038\/cdd.2008.161","article-title":"Neuropeptides kill African trypanosomes by targeting intracellular compartments and inducing autophagic-like cell death","volume":"16","author":"Delgado","year":"2009","journal-title":"Cell Death Differ."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"1817","DOI":"10.1096\/fj.07-096081","article-title":"Human antimicrobial peptide histatin 5 is a cell-penetrating peptide targeting mitochondrial ATP synthesis in Leishmania","volume":"22","author":"Hof","year":"2008","journal-title":"FASEB J."},{"key":"ref_80","unstructured":"Ferguson, M.A.J., Hart, G.W., and Kinoshita, T. (2015). Essentials of Glycobiology, Cold Spring Harbor Laboratory Press. [3rd ed.]."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"84","DOI":"10.2174\/1874421401004010084","article-title":"Structures of glycolipids found in trypanosomatids: contribution to parasite functions","volume":"4","year":"2010","journal-title":"Open Parasitol. J."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"649","DOI":"10.1590\/S0001-37652002000400007","article-title":"The surface charge of trypanosomatids","volume":"74","year":"2002","journal-title":"An. Acad. Bras. Cienc."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"1138","DOI":"10.2174\/138945012802002393","article-title":"Antimicrobial peptide action on parasites","volume":"13","author":"Torrent","year":"2012","journal-title":"Curr. Drug Targets"},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"122","DOI":"10.1128\/MMBR.66.1.122-154.2002","article-title":"Secretory pathway of trypanosomatid parasites","volume":"66","author":"McConville","year":"2002","journal-title":"Microbiol. Mol. Boil. Rev."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"1484","DOI":"10.1111\/j.1365-2958.2006.05459.x","article-title":"The major surface-metalloprotease of the parasitic protozoan, Leishmania, protects against antimicrobial peptide-induced apoptotic killing","volume":"62","author":"Kulkarni","year":"2006","journal-title":"Mol. Microbiol."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"654","DOI":"10.1021\/bi00118a004","article-title":"Solution structure of the lipophosphoglycan of Leishmania donovani","volume":"31","author":"Homans","year":"1992","journal-title":"Biochemistry"},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"114","DOI":"10.6026\/97320630003114","article-title":"Hypothesis Insights from the analysis of a predicted model of gp63 in Leishmania donovani","volume":"3","author":"Razzazan","year":"2008","journal-title":"Bioinformation"},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1128\/AAC.00796-07","article-title":"Comparative analysis of the bactericidal activities of amphibian peptide analogues against multidrug-resistant nosocomial bacterial strains","volume":"52","author":"Mangoni","year":"2008","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"603","DOI":"10.1002\/psc.853","article-title":"Biological characterization and modes of action of temporins and bombinins H, multiple forms of short and mildly cationic anti-microbial peptides from amphibian skin","volume":"13","author":"Mangoni","year":"2007","journal-title":"J. Pept. Sci."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"9258","DOI":"10.1073\/pnas.160257897","article-title":"Lipophosphoglycan is a virulence factor distinct from related glycoconjugates in the protozoan parasite Leishmania major","volume":"97","author":"Epstein","year":"2000","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"194","DOI":"10.1016\/0014-4894(83)90063-2","article-title":"Leishmania mexicana amazonensis: Surface charge of amastigote and promastigote forms","volume":"56","author":"Pimenta","year":"1983","journal-title":"Exp. Parasitol."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1146\/annurev.mi.49.100195.001135","article-title":"The Mechanisms of Trypanosoma cruzi invasion of mammalian cells","volume":"49","author":"Burleigh","year":"1995","journal-title":"Annu. Rev. Microbiol."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"547","DOI":"10.1093\/glycob\/5.6.547","article-title":"Galactofuranose-containing glycoconjugates in trypanosomatids","volume":"5","author":"Colli","year":"1995","journal-title":"Glycobiology"},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"784","DOI":"10.3389\/fmicb.2016.00348","article-title":"Role of Trypanosoma cruzi trans-sialidase on the escape from host immune surveillance","volume":"7","author":"Nardy","year":"2016","journal-title":"Front. Microbiol."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1016\/S0166-6851(01)00245-6","article-title":"The mucin-like glycoprotein super-family of Trypanosoma cruzi: Structure and biological roles","volume":"114","year":"2001","journal-title":"Mol. Biochem. Parasitol."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1128\/IAI.00776-09","article-title":"Major surface protease of trypanosomatids: One size fits all?","volume":"78","author":"Yao","year":"2010","journal-title":"Infect. Immun."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"607","DOI":"10.1093\/glycob\/cwf079","article-title":"The glycoforms of a Trypanosoma brucei variant surface glycoprotein and molecular modeling of a glycosylated surface coat","volume":"12","author":"Mehlert","year":"2002","journal-title":"Glycobiology"},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"369","DOI":"10.1016\/j.mib.2004.05.001","article-title":"Antigenic variation in Trypanosoma brucei: Facts, challenges and mysteries","volume":"7","author":"Pays","year":"2004","journal-title":"Curr. Opin. Microbiol."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/S0166-6851(97)00183-7","article-title":"Expression and function of surface proteins in Trypanosoma brucei","volume":"91","author":"Pays","year":"1998","journal-title":"Mol. Biochem. Parasitol."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1042\/bj2740121","article-title":"Modification of host cell membrane lipid composition by the intra-erythrocytic human malaria parasite Plasmodium falciparum","volume":"274","author":"Hsiao","year":"1991","journal-title":"Biochem. J."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"1713","DOI":"10.1128\/AAC.01342-07","article-title":"The Antimicrobial Peptide NK-2, the Core Region of Mammalian NK-Lysin, Kills Intraerythrocytic Plasmodium falciparum","volume":"52","author":"Gelhaus","year":"2008","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"275","DOI":"10.3389\/fphar.2014.00275","article-title":"Antimicrobial peptides: A new class of antimalarial drugs?","volume":"5","author":"Vale","year":"2014","journal-title":"Front. Pharmacol."},{"key":"ref_103","unstructured":"Weiss, L.M., and Kim, K. (2013). Toxoplasma Gondii: The Model Apicomplexan. Perspectives and Methods, Academic Press. [2nd ed.]."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"11438","DOI":"10.1002\/anie.201203912","article-title":"Chemical Biology of Glycosylphosphatidylinositol Anchors","volume":"51","author":"Tsai","year":"2012","journal-title":"Angew. Chem. Int. Ed."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1111\/j.1365-3024.2011.01294.x","article-title":"Antimicrobial peptide killing of African trypanosomes","volume":"33","author":"Harrington","year":"2011","journal-title":"Parasite Immunol."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"397","DOI":"10.1016\/j.exppara.2010.02.006","article-title":"Interactions of antimicrobial peptides with Leishmania and trypanosomes and their functional role in host parasitism","volume":"126","author":"McGwire","year":"2010","journal-title":"Exp. Parasitol."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"232","DOI":"10.3389\/fmicb.2016.00091","article-title":"Anti-parasitic Peptides from Arthropods and their Application in Drug Therapy","volume":"7","author":"Lacerda","year":"2016","journal-title":"Front. Microbiol."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1124\/pr.55.1.2","article-title":"Mechanisms of Antimicrobial Peptide Action and Resistance","volume":"55","author":"Yeaman","year":"2003","journal-title":"Pharmacol. Rev."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"D933","DOI":"10.1093\/nar\/gkn823","article-title":"APD2: The updated antimicrobial peptide database and its application in peptide design","volume":"37","author":"Wang","year":"2008","journal-title":"Nucleic Acids Res."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"464","DOI":"10.1016\/j.tibtech.2011.05.001","article-title":"The expanding scope of antimicrobial peptide structures and their modes of action","volume":"29","author":"Nguyen","year":"2011","journal-title":"Trends Biotechnol."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"238","DOI":"10.1038\/nrmicro1098","article-title":"Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria?","volume":"3","author":"Brogden","year":"2005","journal-title":"Nat. Rev. Genet."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"14243","DOI":"10.1073\/pnas.1307010110","article-title":"Process of inducing pores in membranes by melittin","volume":"110","author":"Lee","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"1463","DOI":"10.1002\/jcc.23282","article-title":"Modeling peptide binding to anionic membrane pores","volume":"34","author":"He","year":"2013","journal-title":"J. Comput. Chem."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"8846","DOI":"10.1021\/bi0497087","article-title":"Kinetics of Dye Efflux and Lipid Flip-Flop Induced by \u03b4-lysin in phosphatidylcholine vesicles and the mechanism of graded release by amphipathic, \u03b1-helical peptides","volume":"43","author":"Pokorny","year":"2004","journal-title":"Biochemistry"},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"25","DOI":"10.2174\/1568026615666150703121700","article-title":"Antimicrobial peptide structure and mechanism of action: A focus on the role of membrane structure","volume":"16","author":"Lee","year":"2015","journal-title":"Curr. Top. Med. Chem."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"2041","DOI":"10.1016\/j.bbamem.2008.03.020","article-title":"Oxidized phospholipids as potential molecular targets for antimicrobial peptides","volume":"1778","author":"Mattila","year":"2008","journal-title":"Biochim. Biophys. Acta-Biomembr."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1016\/j.bbamem.2010.09.005","article-title":"Indolicidin action on membrane permeability: Carrier mechanism versus pore formation","volume":"1808","author":"Rokitskaya","year":"2011","journal-title":"Biochim. Biophys. Acta-Biomembr."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"2046","DOI":"10.1074\/jbc.272.4.2046","article-title":"Inhibition of Plasmodium falciparum protein synthesis. Targeting the plastid-like organelle with thiostrepton","volume":"272","author":"Rogers","year":"1997","journal-title":"J. Boil. Chem."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1016\/S0014-5793(97)00241-X","article-title":"Thiostrepton binds to malarial plastid rRNA","volume":"406","author":"Clough","year":"1997","journal-title":"FEBS Lett."},{"key":"ref_120","doi-asserted-by":"crossref","unstructured":"Chen, R., Mao, Y., Wang, J., Liu, M., Qiao, Y., Zheng, L., Su, Y., Ke, Q., and Zheng, W. (2018). Molecular mechanisms of an antimicrobial peptide piscidin (Lc-pis) in a parasitic protozoan, Cryptocaryon irritans. BMC Genom., 19.","DOI":"10.1186\/s12864-018-4565-5"},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1016\/S0014-5793(02)02437-7","article-title":"Inhibition of mitochondrial and plastid activity of Plasmodium falciparum by minocycline","volume":"515","author":"Lin","year":"2002","journal-title":"FEBS Lett."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1016\/j.molbiopara.2007.01.005","article-title":"The effects of anti-bacterials on the malaria parasite Plasmodium falciparum","volume":"152","author":"Goodman","year":"2007","journal-title":"Mol. Biochem. Parasitol."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"1338","DOI":"10.1128\/AAC.01096-10","article-title":"Thiostrepton and Derivatives Exhibit Antimalarial and gametocytocidal activity by dually targeting parasite proteasome and apicoplast","volume":"55","author":"Aminake","year":"2011","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"168","DOI":"10.1016\/j.toxicon.2017.08.002","article-title":"Trypanocidal activity of mastoparan from Polybia paulista wasp venom by interaction with TcGAPDH","volume":"137","author":"Vinhote","year":"2017","journal-title":"Toxicon"},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"15496","DOI":"10.1074\/jbc.M809079200","article-title":"Antimicrobial peptide-induced apoptotic death of Leishmania results from calcium-de pendent, caspase-independent mitochondrial toxicity","volume":"284","author":"Kulkarni","year":"2009","journal-title":"J. Biol. Chem."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1016\/S1369-5274(03)00091-2","article-title":"Calcium regulation in protozoan parasites","volume":"6","author":"Moreno","year":"2003","journal-title":"Curr. Opin. Microbiol."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1016\/j.exppara.2005.12.020","article-title":"An intracellular calcium store is present in Leishmania donovani glycosomes","volume":"113","author":"Gupta","year":"2006","journal-title":"Exp. Parasitol."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"2023","DOI":"10.1007\/s00253-015-6375-x","article-title":"Antimicrobial peptides: An alternative for innovative medicines?","volume":"99","author":"Cova","year":"2015","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"ref_129","first-page":"1","article-title":"Combatting bacterial pathogens with immunomodulation and infection tolerance strategies","volume":"16","author":"Fura","year":"2016","journal-title":"Curr. Top. Med. Chem."},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"224","DOI":"10.2174\/1568010033484115","article-title":"Epithelial cell-derived antibacterial peptides human beta-defensins and cathelicidin: Multifunctional activities on mast cells","volume":"2","author":"Niyonsaba","year":"2003","journal-title":"Curr. Drug Targets. Inflamm. Allergy"},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"ii17","DOI":"10.1136\/ard.62.suppl_2.ii17","article-title":"Roles of antimicrobial peptides such as defensins in innate and adaptive immunity","volume":"62","author":"Oppenheim","year":"2003","journal-title":"Ann. Rheum. Dis."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"464","DOI":"10.1016\/j.foodchem.2008.07.086","article-title":"Immunomodulatory effects of marine oligopeptide preparation from Chum Salmon (Oncorhynchus keta) in mice","volume":"113","author":"Yang","year":"2009","journal-title":"Food Chem."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1016\/0278-6915(95)00097-6","article-title":"Antibacterial and immunostimulating casein-derived substances from milk: Casecidin, isracidin peptides","volume":"34","author":"Lahov","year":"1996","journal-title":"Food Chem. Toxicol."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"761","DOI":"10.1038\/nchembio.1393","article-title":"Immune modulation by multifaceted cationic host defense (antimicrobial) peptides","volume":"9","author":"Hilchie","year":"2013","journal-title":"Nat. Methods"},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"7078","DOI":"10.3402\/ehtj.v2i0.7078","article-title":"Host defence peptides: Antimicrobial and immunomodulatory activity and potential applications for tackling antibiotic-resistant infections","volume":"2","author":"Nijnik","year":"2009","journal-title":"Emerg. Heal. Threat. J."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"807","DOI":"10.2174\/138161212799277617","article-title":"Therapeutic potential of host defense peptides in antibiotic-resistant infections","volume":"18","author":"Afacan","year":"2012","journal-title":"Curr. Pharm. Des."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1016\/j.it.2008.12.003","article-title":"AMPed Up immunity: How antimicrobial peptides have multiple roles in immune defense","volume":"30","author":"Lai","year":"2009","journal-title":"Trends Immunol."},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1038\/nrmicro2745","article-title":"Modulating immunity as a therapy for bacterial infections","volume":"10","author":"Hancock","year":"2012","journal-title":"Nat. Rev. Genet."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"35","DOI":"10.2174\/1389203053027494","article-title":"A Re-evaluation of the role of host defence peptides in mammalian immunity","volume":"6","author":"Bowdish","year":"2005","journal-title":"Curr. Protein Pept. Sci."},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1177\/1753425918821168","article-title":"Glycoconjugates of Gram-negative bacteria and parasitic protozoa\u2014Are they similar in orchestrating the innate immune response?","volume":"25","author":"Janczarek","year":"2019","journal-title":"Innate Immun."},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"135ra64","DOI":"10.1126\/scitranslmed.3003515","article-title":"Effective adjunctive therapy by an innate defense regulatory peptide in a preclinical model of severe malaria","volume":"4","author":"Achtman","year":"2012","journal-title":"Sci. Transl. Med."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"965","DOI":"10.1128\/AAC.47.3.965-971.2003","article-title":"Modulation of the activity of secretory phospholipase A2 by antimicrobial peptides","volume":"47","author":"Zhao","year":"2003","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"246","DOI":"10.1016\/j.exppara.2008.02.002","article-title":"The effects of bee (Apis mellifera) venom phospholipase A2 on Trypanosoma brucei brucei and enterobacteria","volume":"119","author":"Boutrin","year":"2008","journal-title":"Exp. Parasitol."},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"571","DOI":"10.1016\/j.ijbiomac.2017.04.013","article-title":"BmajPLA 2-II, a basic Lys49-phospholipase A2 homologue from Bothrops marajoensis snake venom with parasiticidal potential","volume":"102","author":"Grabner","year":"2017","journal-title":"Int. J. Boil. Macromol."},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"537","DOI":"10.1186\/s40409-015-0049-0","article-title":"In vitro activity of phospholipase A2 and of peptides from Crotalus durissus terrificus venom against amastigote and promastigote forms of Leishmania (L.) infantum chagasi","volume":"21","author":"Barros","year":"2015","journal-title":"J. Venom. Anim. Toxins Incl. Trop. Dis."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1111\/j.1749-6632.2010.05787.x","article-title":"Immunomodulators as adjuvants for vaccines and antimicrobial therapy","volume":"1213","author":"Nicholls","year":"2010","journal-title":"Ann. N. Y. Acad. Sci."},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1186\/1756-3305-7-317","article-title":"The history of Chagas disease","volume":"7","author":"Steverding","year":"2014","journal-title":"Parasit. Vectors"},{"key":"ref_148","unstructured":"(2019, June 25). Centers for Disease Control and Prevention; Global Health, D. of P.D. and M. CDC\u2014American trypanosomiasis, Available online: https:\/\/www.cdc.gov\/parasites."},{"key":"ref_149","unstructured":"World Health Organization (2019, June 25). WHO Chagas disease (American trypanosomiasis). Available online: https:\/\/www.who.int\/chagas\/en\/."},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1016\/j.ejim.2017.05.001","article-title":"Chagas disease in Europe: A review for the internist in the globalized world","volume":"43","author":"Antinori","year":"2017","journal-title":"Eur. J. Intern. Med."},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"82","DOI":"10.1016\/S0140-6736(17)31612-4","article-title":"Chagas disease","volume":"391","author":"Molina","year":"2018","journal-title":"Lancet"},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.actatropica.2015.12.017","article-title":"Current drug therapy and pharmaceutical challenges for Chagas disease","volume":"156","author":"Bermudez","year":"2016","journal-title":"Acta Trop."},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1016\/j.ijpharm.2014.06.015","article-title":"Development of novel benznidazole formulations: Physicochemical characterization and in vivo evaluation on parasitemia reduction in Chagas disease","volume":"472","author":"Escario","year":"2014","journal-title":"Int. J. Pharm."},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"220","DOI":"10.1093\/infdis\/jis331","article-title":"Benznidazole-Resistance in Trypanosoma cruzi is a readily acquired trait that can arise independently in a single population","volume":"206","author":"Mejia","year":"2012","journal-title":"J. Infect. Dis."},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1016\/j.toxicon.2013.03.011","article-title":"Melittin peptide kills Trypanosoma cruzi parasites by inducing different cell death pathways","volume":"69","author":"Adade","year":"2013","journal-title":"Toxicon"},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"1444","DOI":"10.1017\/S0031182012000790","article-title":"Apis mellifera venom induces different cell death pathways in Trypanosoma cruzi","volume":"139","author":"Adade","year":"2012","journal-title":"Parasitology"},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1016\/0166-6851(96)02707-7","article-title":"Calcium influx in Trypanosoma brucei can be induced by amphiphilic peptides and amines","volume":"81","author":"Ruben","year":"1996","journal-title":"Mol. Biochem. Parasitol."},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"2441","DOI":"10.1128\/AAC.45.9.2441-2449.2001","article-title":"N-terminal fatty acid substitution increases the leishmanicidal activity of CA(1-7)M(2-9), a cecropin-melittin hybrid peptide","volume":"45","author":"Chicharro","year":"2001","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_159","first-page":"323","article-title":"Antimicrobial activity of an antimicrobial peptide against amastigote forms of Leishmania major","volume":"9","author":"Khalili","year":"2018","journal-title":"Veter-Res. Forum Int. Q. J."},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"342","DOI":"10.1016\/j.exppara.2010.02.016","article-title":"Trypanosoma cruzi: Synergistic cytotoxicity of multiple amphipathic anti-microbial peptides to T. cruzi and potential bacterial hosts","volume":"125","author":"Fieck","year":"2010","journal-title":"Exp. Parasitol."},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1515\/hsz-2017-0198","article-title":"The dinoponeratoxin peptides from the giant ant Dinoponera quadriceps display in vitro antitrypanosomal activity","volume":"399","author":"Lima","year":"2018","journal-title":"Boil. Chem."},{"key":"ref_162","doi-asserted-by":"crossref","unstructured":"Parente, A.M.S., Daniele-Silva, A., Furtado, A.A., Melo, M.A., Lacerda, A.F., Queiroz, M., Moreno, C., Santos, E., Rocha, H.A.O., and Barbosa, E.G. (2018). Analogs of the scorpion venom peptide Stigmurin: Structural assessment, toxicity, and increased antimicrobial activity. Toxins, 10.","DOI":"10.3390\/toxins10040161"},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1007\/s00726-009-0471-0","article-title":"Cupiennin 1a exhibits a remarkably broad, non-stereospecific cytolytic activity on bacteria, protozoan parasites, insects, and human cancer cells","volume":"40","author":"Willems","year":"2011","journal-title":"Amino Acids"},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"448","DOI":"10.1038\/nature20137","article-title":"Alternative modes of client binding enable functional plasticity of Hsp70","volume":"539","author":"Mashaghi","year":"2016","journal-title":"Nature"},{"key":"ref_165","doi-asserted-by":"crossref","first-page":"3016","DOI":"10.1021\/bi002656a","article-title":"The antibacterial peptide pyrrhocoricin inhibits the atpase actions of DnaK and prevents chaperone-assisted protein folding","volume":"40","author":"Kragol","year":"2001","journal-title":"Biochemistry"},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"941","DOI":"10.1038\/nrd2144","article-title":"Innovative lead discovery strategies for tropical diseases","volume":"5","author":"Nwaka","year":"2006","journal-title":"Nat. Rev. Drug Discov."},{"key":"ref_167","doi-asserted-by":"crossref","unstructured":"Amorim-Carmo, B., Daniele-Silva, A., Parente, A.M.S., Furtado, A.A., Carvalho, E., Oliveira, J.W.F., Santos, E.C.G., Silva, M.S., Silva, S.R.B., and Silva-J\u00fanior, A.A. (2019). Potent and broad-spectrum antimicrobial activity of analogs from the scorpion peptide stigmurin. Int. J. Mol. Sci., 20.","DOI":"10.3390\/ijms20030623"},{"key":"ref_168","unstructured":"World Health Organization (2019, July 08). WHO Trypanosomiasis, Human African (Sleeping Sickness). Available online: https:\/\/www.who.int\/news-room\/fact-sheets\/detail\/trypanosomiasis-human-african-(sleeping-sickness)."},{"key":"ref_169","doi-asserted-by":"crossref","first-page":"575","DOI":"10.1038\/nrmicro3298","article-title":"The molecular arms race between African trypanosomes and humans","volume":"12","author":"Pays","year":"2014","journal-title":"Nat. Rev. Genet."},{"key":"ref_170","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1002\/prca.201700041","article-title":"Sleeping Sickness in the \u2018Omics Era","volume":"12","author":"Tiberti","year":"2018","journal-title":"Proteom.-Clin. Appl."},{"key":"ref_171","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1038\/nature.2017.22856","article-title":"Pill treats sleeping sickness Scientists seek approval from regulators for this relatively quick and easy therapy","volume":"550","author":"Maxmen","year":"2017","journal-title":"Nature"},{"key":"ref_172","doi-asserted-by":"crossref","first-page":"727","DOI":"10.1038\/nrd1824","article-title":"Opportunities and Challenges in Antiparasitic Drug Discovery","volume":"4","author":"Pink","year":"2005","journal-title":"Nat. Rev. Drug Discov."},{"key":"ref_173","unstructured":"World Health Organization (2019, July 23). WHO Leishmaniasis. Available online: https:\/\/www.who.int\/en\/news-room\/fact-sheets\/detail\/leishmaniasis."},{"key":"ref_174","unstructured":"Myler, P.J., and Fasel, N. (2008). Leishmania: After the Genome, Caister Academic."},{"key":"ref_175","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1093\/qjmed\/hct116","article-title":"Leishmaniasis: Clinical syndromes and treatment","volume":"107","author":"McGwire","year":"2014","journal-title":"QJM"},{"key":"ref_176","doi-asserted-by":"crossref","unstructured":"Alvar, J., Velez, I.D., Bern, C., Herrero, M., Desjeux, P., Cano, J., Jannin, J., and Boer, M.D. (2012). Leishmaniasis worldwide and global estimates of its incidence. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0035671"},{"key":"ref_177","doi-asserted-by":"crossref","first-page":"604","DOI":"10.1038\/nrmicro2608","article-title":"Leishmaniasis: Complexity at the host\u2013pathogen interface","volume":"9","author":"Kaye","year":"2011","journal-title":"Nat. Rev. Genet."},{"key":"ref_178","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1080\/14787210.2018.1483720","article-title":"Prospects for antimicrobial peptide-based immunotherapy approaches in Leishmania control","volume":"16","author":"Zahedifard","year":"2018","journal-title":"Expert Rev. Anti-Infect. Ther."},{"key":"ref_179","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1016\/0035-9203(93)90140-L","article-title":"The treatment of kala-azar in the Sudan with sodium stibogluconate: A randomized trial of three dosage regimens","volume":"87","author":"Ali","year":"1993","journal-title":"Trans. R. Soc. Trop. Med. Hyg."},{"key":"ref_180","doi-asserted-by":"crossref","first-page":"2603","DOI":"10.1021\/jm900185q","article-title":"Molecular basis of antimony treatment in leishmaniasis","volume":"52","author":"Baiocco","year":"2009","journal-title":"J. Med. Chem."},{"key":"ref_181","doi-asserted-by":"crossref","first-page":"557","DOI":"10.1517\/14656560903555219","article-title":"Cutaneous and mucocutaneous leishmaniasis: Emerging therapies and progress in disease management","volume":"11","author":"Ameen","year":"2010","journal-title":"Expert Opin. Pharmacother."},{"key":"ref_182","doi-asserted-by":"crossref","first-page":"1375","DOI":"10.1086\/503371","article-title":"Resistance to Antimony and Treatment Failure in Human Leishmania (Viannia) Infection","volume":"193","author":"Rojas","year":"2006","journal-title":"J. Infect. Dis."},{"key":"ref_183","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1128\/CMR.19.1.111-126.2006","article-title":"Drug resistance in leishmaniasis","volume":"19","author":"Croft","year":"2006","journal-title":"Clin. Microbiol. Rev."},{"key":"ref_184","first-page":"815023","article-title":"Advances in development of new treatment for leishmaniasis","volume":"2015","author":"Guedes","year":"2015","journal-title":"Biomed Res. Int."},{"key":"ref_185","doi-asserted-by":"crossref","first-page":"1337","DOI":"10.1517\/13543784.14.11.1337","article-title":"Clinical status of agents being developed for leishmaniasis","volume":"14","author":"Berman","year":"2005","journal-title":"Expert Opin. Investig. Drugs"},{"key":"ref_186","first-page":"733","article-title":"Miltefosine in the treatment of leishmaniasis: Clinical evidence for informed clinical risk management","volume":"3","author":"Sundar","year":"2007","journal-title":"Ther. Clin. Risk Manag."},{"key":"ref_187","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1016\/j.bbrc.2011.11.023","article-title":"A novel mechanism for an old drug: Amphotericin B in the treatment of visceral leishmaniasis","volume":"416","author":"Chattopadhyay","year":"2011","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_188","doi-asserted-by":"crossref","first-page":"1000","DOI":"10.1086\/591972","article-title":"New treatment approach in indian visceral leishmaniasis: Single-dose liposomal amphotericin b followed by short-course oral miltefosine","volume":"47","author":"Sundar","year":"2008","journal-title":"Clin. Infect. Dis."},{"key":"ref_189","doi-asserted-by":"crossref","first-page":"33464","DOI":"10.1074\/jbc.M001491200","article-title":"Isolation and characterization of gomesin, an 18-residue cysteine-rich defense peptide from the spider Acanthoscurria gomesiana hemocytes with sequence similarities to horseshoe crab antimicrobial peptides of the tachyplesin family","volume":"275","author":"Silva","year":"2000","journal-title":"J. Biol. Chem."},{"key":"ref_190","doi-asserted-by":"crossref","first-page":"318","DOI":"10.1016\/j.molbiopara.2006.09.004","article-title":"Differentiation of Leishmania major is impaired by over-expression of pyroglutamyl peptidase I","volume":"150","author":"Schaeffer","year":"2006","journal-title":"Mol. Biochem. Parasitol."},{"key":"ref_191","doi-asserted-by":"crossref","first-page":"2320","DOI":"10.1016\/j.peptides.2007.09.017","article-title":"Decoralin, a novel linear cationic \u03b1-helical peptide from the venom of the solitary eumenine wasp Oreumenes decoratus","volume":"28","author":"Konno","year":"2007","journal-title":"Peptides"},{"key":"ref_192","doi-asserted-by":"crossref","first-page":"2624","DOI":"10.1016\/j.peptides.2006.04.013","article-title":"Eumenitin, a novel antimicrobial peptide from the venom of the solitary eumenine wasp Eumenes rubronotatus","volume":"27","author":"Konno","year":"2006","journal-title":"Peptides"},{"key":"ref_193","doi-asserted-by":"crossref","first-page":"1505","DOI":"10.1016\/S0041-0101(00)00083-0","article-title":"Structure and biological activities of eumenine mastoparan-AF (EMP-AF), a new mast cell degranulating peptide in the venom of the solitary wasp (Anterhynchium flavomarginatum micado)","volume":"38","author":"Konno","year":"2000","journal-title":"Toxicon"},{"key":"ref_194","doi-asserted-by":"crossref","first-page":"1081","DOI":"10.1016\/j.toxicon.2011.04.014","article-title":"Chemical and biological characterization of four new linear cationic \u03b1-helical peptides from the venoms of two solitary eumenine wasps","volume":"57","author":"Rangel","year":"2011","journal-title":"Toxicon"},{"key":"ref_195","doi-asserted-by":"crossref","first-page":"683","DOI":"10.1016\/j.peptides.2011.01.011","article-title":"Leishmanicidal activity of synthetic antimicrobial peptides in an infection model with human dendritic cells","volume":"32","author":"Lozano","year":"2011","journal-title":"Peptides"},{"key":"ref_196","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1042\/bj3300453","article-title":"The plasma membrane of Leishmania donovani promastigotes is the main target for CA(1\u20138)M(1\u201318), a synthetic cecropin A\u2013melittin hybrid peptide","volume":"330","author":"Ubach","year":"1998","journal-title":"Biochem. J."},{"key":"ref_197","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1016\/j.peptides.2016.04.001","article-title":"Biochemical and biophysical combined study of bicarinalin, an ant venom antimicrobial peptide","volume":"79","author":"Berger","year":"2016","journal-title":"Peptides"},{"key":"ref_198","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1007\/s00436-006-0133-z","article-title":"In vitro leishmanicidal activity of Tityus discrepans scorpion venom","volume":"99","author":"Borges","year":"2006","journal-title":"Parasitol. Res."},{"key":"ref_199","doi-asserted-by":"crossref","first-page":"128","DOI":"10.1016\/j.toxicon.2016.08.008","article-title":"Antiparasitic effect of Dinoponera quadriceps giant ant venom","volume":"120","author":"Lima","year":"2016","journal-title":"Toxicon"},{"key":"ref_200","doi-asserted-by":"crossref","first-page":"641","DOI":"10.1128\/AAC.48.2.641-643.2004","article-title":"Safety and efficacy of antimicrobial peptides against naturally acquired leishmaniasis","volume":"48","author":"Alberola","year":"2004","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_201","doi-asserted-by":"crossref","first-page":"723","DOI":"10.1016\/S0140-6736(13)60024-0","article-title":"Malaria","volume":"383","author":"White","year":"2014","journal-title":"Lancet"},{"key":"ref_202","doi-asserted-by":"crossref","first-page":"1155","DOI":"10.1007\/s11538-017-0276-3","article-title":"A Malaria transmission model with temperature-dependent incubation period","volume":"72","author":"Wang","year":"2017","journal-title":"Bull. Math. Boil."},{"key":"ref_203","doi-asserted-by":"crossref","unstructured":"Watson, J., Taylor, W.R.J., Bancone, G., Chu, C.S., Jittamala, P., and White, N.J. (2018). Implications of current therapeutic restrictions for primaquine and tafenoquine in the radical cure of vivax malaria. PLoS Negl. Trop. Dis., 12.","DOI":"10.1371\/journal.pntd.0006440"},{"key":"ref_204","doi-asserted-by":"crossref","first-page":"1637","DOI":"10.1093\/infdis\/jit077","article-title":"Malaria transmission after artemether-lumefantrine and dihydroartemisinin-piperaquine: A randomized trial","volume":"207","author":"Sawa","year":"2013","journal-title":"J. Infect. Dis."},{"key":"ref_205","first-page":"583","article-title":"Malaria chemoprophylaxis and travel immunizations","volume":"82","author":"Jones","year":"2010","journal-title":"Am. Fam. Physician"},{"key":"ref_206","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1016\/S0014-5793(00)01384-3","article-title":"Scorpine, an anti-malaria and anti-bacterial agent purified from scorpion venom","volume":"471","author":"Conde","year":"2000","journal-title":"FEBS Lett."},{"key":"ref_207","doi-asserted-by":"crossref","first-page":"350","DOI":"10.1016\/j.biochi.2010.01.011","article-title":"Characterization of two linear cationic antimalarial peptides in the scorpion Mesobuthus eupeus","volume":"92","author":"Gao","year":"2010","journal-title":"Biochimie"},{"key":"ref_208","doi-asserted-by":"crossref","first-page":"12630","DOI":"10.1073\/pnas.221466798","article-title":"Gambicin: A novel immune responsive antimicrobial peptide from the malaria vector Anopheles gambiae","volume":"98","author":"Vizioli","year":"2001","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_209","doi-asserted-by":"crossref","first-page":"872","DOI":"10.1016\/j.bbapap.2009.12.017","article-title":"MeuTXK\u03b21, a scorpion venom-derived two-domain potassium channel toxin-like peptide with cytolytic activity","volume":"1804","author":"Zhu","year":"2010","journal-title":"Biochim. Biophys. Acta-Proteins Proteom."},{"key":"ref_210","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1016\/j.febslet.2004.07.019","article-title":"Isolation and characterization of Psalmopeotoxin I and II: Two novel antimalarial peptides from the venom of the tarantula Psalmopoeus cambridgei","volume":"572","author":"Choi","year":"2004","journal-title":"FEBS Lett."},{"key":"ref_211","doi-asserted-by":"crossref","first-page":"442","DOI":"10.1021\/acsinfecdis.6b00045","article-title":"Contribution of amphipathicity and hydrophobicity to the antimicrobial activity and cytotoxicity of \u03b2-hairpin peptides","volume":"2","author":"Edwards","year":"2016","journal-title":"ACS Infect. Dis."},{"key":"ref_212","doi-asserted-by":"crossref","first-page":"346","DOI":"10.1016\/j.exppara.2007.01.022","article-title":"Effect of the antimicrobial peptide Gomesin against different life stages of Plasmodium spp.","volume":"116","author":"Moreira","year":"2007","journal-title":"Exp. Parasitol."},{"key":"ref_213","doi-asserted-by":"crossref","unstructured":"Carter, V., Underhill, A., Baber, I., Sylla, L., Baby, M., Larget-Thiery, I., Zettor, A., Bourgouin, C., Langel, \u00dc., and Faye, I. (2013). Killer bee molecules: antimicrobial peptides as effector molecules to target sporogonic stages of Plasmodium. PLoS Pathog., 9.","DOI":"10.1371\/journal.ppat.1003790"},{"key":"ref_214","first-page":"2954","article-title":"Antiplasmodial activity is an ancient and conserved feature of tick defensins","volume":"7","author":"Tonk","year":"2016","journal-title":"Front. Microbiol."},{"key":"ref_215","doi-asserted-by":"crossref","first-page":"146","DOI":"10.1016\/j.gene.2014.03.002","article-title":"Identification and partial characterisation of new members of the Ixodes ricinus defensin family","volume":"540","author":"Tonk","year":"2014","journal-title":"Gene"},{"key":"ref_216","doi-asserted-by":"crossref","first-page":"55042","DOI":"10.1074\/jbc.M408881200","article-title":"Dissection of antibacterial and toxic activity of melittin","volume":"279","author":"Asthana","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_217","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1016\/S0167-4838(01)00271-0","article-title":"Anoplin, a novel antimicrobial peptide from the venom of the solitary wasp Anoplius samariensis","volume":"1550","author":"Konno","year":"2001","journal-title":"Biochim. Biophys. Acta-Protein Struct. Mol. Enzym."},{"key":"ref_218","doi-asserted-by":"crossref","first-page":"1942","DOI":"10.1248\/cpb.27.1942","article-title":"A new mast cell degranulating peptide \u201cmastoparan\u201d in the venom of Vespula lewisii","volume":"27","author":"Hirai","year":"1979","journal-title":"Chem. Pharm. Bull."},{"key":"ref_219","doi-asserted-by":"crossref","first-page":"715","DOI":"10.1016\/j.parint.2018.07.004","article-title":"Congenital toxoplasmosis: An overview of the neurological and ocular manifestations","volume":"67","author":"Khan","year":"2018","journal-title":"Parasitol. Int."},{"key":"ref_220","doi-asserted-by":"crossref","first-page":"294","DOI":"10.1016\/j.exppara.2012.12.011","article-title":"Toxoplasma gondii: The effect of fluconazole combined with sulfadiazine and pyrimethamine against acute toxoplasmosis in murine model","volume":"133","author":"Vommaro","year":"2013","journal-title":"Exp. Parasitol."},{"key":"ref_221","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1016\/j.exppara.2019.01.009","article-title":"Anti-parasitic effect on Toxoplasma gondii induced by a spider peptide lycosin-I","volume":"198","author":"Tang","year":"2019","journal-title":"Exp. Parasitol."},{"key":"ref_222","first-page":"3633","article-title":"tick longicin implicated in the arthropod transmission of Toxoplasma Gondii","volume":"3","author":"Tanaka","year":"2012","journal-title":"J. Vet. Sci. Technol."},{"key":"ref_223","doi-asserted-by":"crossref","first-page":"3633","DOI":"10.1128\/IAI.00256-07","article-title":"Babesial vector tick defensin against Babesia sp. Parasites","volume":"75","author":"Tsuji","year":"2007","journal-title":"Infect. Immun."},{"key":"ref_224","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1016\/j.toxicon.2017.02.020","article-title":"Insects, arachnids and centipedes venom: A powerful weapon against bacteria. A literature review","volume":"130","author":"Fratini","year":"2017","journal-title":"Toxicon"},{"key":"ref_225","doi-asserted-by":"crossref","first-page":"1119","DOI":"10.2174\/1568026616666160930151242","article-title":"Animal venom peptides: potential for new antimicrobial agents","volume":"17","author":"Macedo","year":"2017","journal-title":"Curr. Top. Med. Chem."},{"key":"ref_226","doi-asserted-by":"crossref","unstructured":"Rajamuthiah, R., Jayamani, E., Conery, A.L., Fuchs, B.B., Kim, W., Johnston, T., Vilcinskas, A., Ausubel, F.M., and Mylonakis, E. (2015). A defensin from the model beetle Tribolium castaneum acts synergistically with telavancin and daptomycin against multidrug resistant Staphylococcus aureus. PLoS ONE, 10.","DOI":"10.1371\/journal.pone.0128576"},{"key":"ref_227","doi-asserted-by":"crossref","first-page":"6973","DOI":"10.1007\/s00253-014-5728-1","article-title":"Expression and purification of cyto-insectotoxin (Cit1a) using silkworm larvae targeting for an antimicrobial therapeutic agent","volume":"98","author":"Ali","year":"2014","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"ref_228","doi-asserted-by":"crossref","first-page":"1957","DOI":"10.1016\/j.peptides.2010.08.008","article-title":"Cost-effective expression and purification of antimicrobial and host defense peptides in Escherichia coli","volume":"31","author":"Bommarius","year":"2010","journal-title":"Peptides"},{"key":"ref_229","doi-asserted-by":"crossref","first-page":"260","DOI":"10.1016\/j.pep.2011.08.001","article-title":"Recombinant production of antimicrobial peptides in Escherichia coli: A review","volume":"80","author":"Li","year":"2011","journal-title":"Protein Expr. Purif."},{"key":"ref_230","doi-asserted-by":"crossref","first-page":"1971","DOI":"10.1007\/s00436-014-3847-3","article-title":"Design of protease-resistant pexiganan enhances antileishmanial activity","volume":"113","author":"Kulkarni","year":"2014","journal-title":"Parasitol. Res."},{"key":"ref_231","doi-asserted-by":"crossref","first-page":"1537","DOI":"10.1086\/593185","article-title":"Topical versus systemic antimicrobial therapy for treating mildly infected diabetic foot ulcers: A randomized, controlled, double-blinded, multicenter trial of pexiganan cream","volume":"47","author":"Lipsky","year":"2008","journal-title":"Clin. Infect. Dis."},{"key":"ref_232","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1038\/nbt.2572","article-title":"Antimicrobial peptides stage a comeback","volume":"31","author":"Fox","year":"2013","journal-title":"Nat. Biotechnol."},{"key":"ref_233","unstructured":"World Health Organization (2019, July 28). WHO Malaria. Available online: https:\/\/www.who.int\/malaria\/en\/."},{"key":"ref_234","doi-asserted-by":"crossref","unstructured":"(2018). Wanted: A reward for antibiotic development. Nat. Biotechnol., 36, 555.","DOI":"10.1038\/nbt.4193"}],"container-title":["Toxins"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2072-6651\/11\/10\/563\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T13:24:09Z","timestamp":1760189049000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2072-6651\/11\/10\/563"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,9,25]]},"references-count":234,"journal-issue":{"issue":"10","published-online":{"date-parts":[[2019,10]]}},"alternative-id":["toxins11100563"],"URL":"https:\/\/doi.org\/10.3390\/toxins11100563","relation":{},"ISSN":["2072-6651"],"issn-type":[{"value":"2072-6651","type":"electronic"}],"subject":[],"published":{"date-parts":[[2019,9,25]]}}}