{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,11]],"date-time":"2026-07-11T07:14:20Z","timestamp":1783754060383,"version":"3.55.0"},"reference-count":40,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2026,8,1]],"date-time":"2026-08-01T00:00:00Z","timestamp":1785542400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,8,1]],"date-time":"2026-08-01T00:00:00Z","timestamp":1785542400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2026,8,1]],"date-time":"2026-08-01T00:00:00Z","timestamp":1785542400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2026,8,1]],"date-time":"2026-08-01T00:00:00Z","timestamp":1785542400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2026,8,1]],"date-time":"2026-08-01T00:00:00Z","timestamp":1785542400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2026,8,1]],"date-time":"2026-08-01T00:00:00Z","timestamp":1785542400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2026,8,1]],"date-time":"2026-08-01T00:00:00Z","timestamp":1785542400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Microbial Pathogenesis"],"published-print":{"date-parts":[[2026,8]]},"DOI":"10.1016\/j.micpath.2026.108550","type":"journal-article","created":{"date-parts":[[2026,5,12]],"date-time":"2026-05-12T02:25:14Z","timestamp":1778552714000},"page":"108550","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":0,"special_numbering":"C","title":["Rational engineering of a novel cationic LL-37\u2013temporin SHa hybrid peptide with anti-parasitic activity and effects on mitochondrial membrane potential in protozoan parasites"],"prefix":"10.1016","volume":"217","author":[{"given":"Kiran","family":"Khurshid","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1204-5930","authenticated-orcid":false,"given":"Muhammad Adnan Sabir","family":"Mughal","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jamal Muhammad","family":"Khan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zubair Azhar","family":"Nomi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Baseer","family":"Ahmad","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Haizhou","family":"Gong","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.micpath.2026.108550_bib1","doi-asserted-by":"crossref","first-page":"96","DOI":"10.1186\/s40249-024-01260-x","article-title":"Prevalence and attributable health burdens of vector-borne parasitic infectious diseases of poverty, 1990--2021: findings from the global burden of disease study 2021","volume":"13","author":"Zhu","year":"2024","journal-title":"Infect. Dis. Poverty"},{"key":"10.1016\/j.micpath.2026.108550_bib2","series-title":"Nanostructured Drug Deliv. Syst. Infect. Dis. Treat.","first-page":"1","article-title":"Infectious diseases and its global epidemiology","author":"Baral","year":"2024"},{"key":"10.1016\/j.micpath.2026.108550_bib3","first-page":"2747","article-title":"Progress in redirecting antiparasitic drugs for cancer treatment","author":"Huang","year":"2021","journal-title":"Drug Des. Dev. Ther."},{"key":"10.1016\/j.micpath.2026.108550_bib4","doi-asserted-by":"crossref","first-page":"1419","DOI":"10.1039\/D5NP00007F","article-title":"Natural products in antiparasitic drug discovery: advances, opportunities and challenges","volume":"42","author":"Shang","year":"2025","journal-title":"Nat. Prod. Rep."},{"key":"10.1016\/j.micpath.2026.108550_bib5","doi-asserted-by":"crossref","first-page":"262","DOI":"10.1038\/s41579-023-00993-0","article-title":"Alternative therapeutic strategies to treat antibiotic-resistant pathogens","volume":"22","author":"MacNair","year":"2024","journal-title":"Nat. Rev. Microbiol."},{"key":"10.1016\/j.micpath.2026.108550_bib6","doi-asserted-by":"crossref","first-page":"402","DOI":"10.3390\/ph18030402","article-title":"Combating antibiotic resistance: mechanisms, multidrug-resistant pathogens, and novel therapeutic approaches: an updated review","volume":"18","author":"Elshobary","year":"2025","journal-title":"Pharmaceuticals"},{"key":"10.1016\/j.micpath.2026.108550_bib7","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1016\/j.pt.2023.02.004","article-title":"Helminthic host defense peptides: using the parasite to defend the host","volume":"39","author":"Mladineo","year":"2023","journal-title":"Trends Parasitol."},{"key":"10.1016\/j.micpath.2026.108550_bib8","doi-asserted-by":"crossref","first-page":"122","DOI":"10.1007\/s00436-024-08133-0","article-title":"Therapeutic potential of antimicrobial peptides against pathogenic protozoa","volume":"123","author":"Hagemann","year":"2024","journal-title":"Parasitol. Res."},{"key":"10.1016\/j.micpath.2026.108550_bib9","doi-asserted-by":"crossref","DOI":"10.1128\/mmbr.00037-22","article-title":"Antimicrobial peptides and small molecules targeting the cell membrane of Staphylococcus aureus","volume":"87","author":"Ganesan","year":"2023","journal-title":"Microbiol. Mol. Biol. Rev."},{"key":"10.1016\/j.micpath.2026.108550_bib10","doi-asserted-by":"crossref","first-page":"1174","DOI":"10.3390\/polym17091174","article-title":"Polymer micelles as nanocarriers of bioactive peptides","volume":"17","author":"Petrov","year":"2025","journal-title":"Polymers"},{"key":"10.1016\/j.micpath.2026.108550_bib11","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1042\/ETLS20220089","article-title":"The enemy within: lipid asymmetry in intracellular parasite--host interactions","volume":"7","author":"Fraser","year":"2023","journal-title":"Emerg. Top. Life Sci."},{"key":"10.1016\/j.micpath.2026.108550_bib12","doi-asserted-by":"crossref","DOI":"10.1016\/j.peptides.2023.171011","article-title":"The LL-37 domain: a clue to cathelicidin immunomodulatory response?","volume":"165","author":"Leite","year":"2023","journal-title":"Peptides"},{"key":"10.1016\/j.micpath.2026.108550_bib13","series-title":"Deciphering the Role of ARK5 and Hnrnp A1 in Regulating the Osmotic Stress","author":"Bhattarai","year":"2024"},{"key":"10.1016\/j.micpath.2026.108550_bib14","doi-asserted-by":"crossref","first-page":"8103","DOI":"10.3390\/ijms26168103","article-title":"Antimicrobial peptides of the cathelicidin family: Focus on LL-37 and its modifications","volume":"26","author":"Voronko","year":"2025","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.micpath.2026.108550_bib15","doi-asserted-by":"crossref","first-page":"3145","DOI":"10.1021\/acsbiomaterials.4c02029","article-title":"Exploring the antimicrobial potential of LL-37 derivatives: recent developments and challenges","volume":"11","author":"Yuan","year":"2025","journal-title":"ACS Biomater. Sci. Eng."},{"key":"10.1016\/j.micpath.2026.108550_bib16","first-page":"587","article-title":"Recent advancement in novel wound healing therapies by using antimicrobial peptides derived from humans and amphibians, curr. Protein pept","volume":"25","author":"Satapathy","year":"2024","journal-title":"Sci."},{"key":"10.1016\/j.micpath.2026.108550_bib17","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1007\/s10989-024-10626-6","article-title":"Nature-derived peptides as promising antiparasitic agents against neglected tropical diseases","volume":"30","author":"Lim","year":"2024","journal-title":"Int. J. Pept. Res. Therapeut."},{"key":"10.1016\/j.micpath.2026.108550_bib18","doi-asserted-by":"crossref","DOI":"10.1002\/macp.202200226","article-title":"Design of antimicrobial polymers","volume":"224","author":"Pham","year":"2023","journal-title":"Macromol. Chem. Phys."},{"key":"10.1016\/j.micpath.2026.108550_bib19","article-title":"An optimized 2, 2\u2019-dipicolylamine-rutaecarpine quaternary ammonium derivative: targeting bacterial membrane disruption for enhanced anti-methicillin-resistant Staphylococcus aureus (MRSA) activity","author":"Xu","year":"2025","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.micpath.2026.108550_bib20","doi-asserted-by":"crossref","DOI":"10.1002\/pep2.24343","article-title":"Review on therapeutic potential of peptides: advancements in synthesis methods, linear and cyclic peptides, and strategies for overcoming challenges","volume":"116","author":"Lalani","year":"2024","journal-title":"Pept. Sci."},{"key":"10.1016\/j.micpath.2026.108550_bib21","doi-asserted-by":"crossref","first-page":"15277","DOI":"10.2147\/IJN.S569237","article-title":"Molecular-level design principles and strategies of peptide self-assembly nanomaterials: from sequence engineering to functional applications","author":"Luo","year":"2025","journal-title":"Int. J. Nanomed."},{"key":"10.1016\/j.micpath.2026.108550_bib22","doi-asserted-by":"crossref","first-page":"2385","DOI":"10.2174\/0115680266350153250121072651","article-title":"The functional mechanism and structure-activity relationship of antibacterial peptides","volume":"25","author":"Zhong","year":"2025","journal-title":"Curr. Top. Med. Chem."},{"key":"10.1016\/j.micpath.2026.108550_bib23","article-title":"Antimicrobial peptides: natural templates for next-generation therapeutics against antimicrobial resistance","volume":"15","author":"Ngashangva","year":"2025","journal-title":"Front. Cell. Infect. Microbiol."},{"key":"10.1016\/j.micpath.2026.108550_bib24","article-title":"From membrane composition to antimicrobial strategies: experimental and computational approaches to AMP design and selectivity","author":"Rossetti","year":"2025","journal-title":"Small"},{"key":"10.1016\/j.micpath.2026.108550_bib25","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2025.108298","article-title":"Others, antimicrobial peptides selectively target malaria parasites by a cholesterol-dependent mechanism","volume":"301","author":"Kiper","year":"2025","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.micpath.2026.108550_bib26","article-title":"Others, ADVANCEMENTS IN PEPTIDE-BASED THERAPEUTICS: design, synthesis and clinical applications","volume":"23","author":"Arora","year":"2023","journal-title":"Biochem. Cell. Arch."},{"key":"10.1016\/j.micpath.2026.108550_bib27","doi-asserted-by":"crossref","first-page":"227","DOI":"10.3390\/pharmaceutics16020227","article-title":"The potential use of peptides in the fight against chagas disease and leishmaniasis","volume":"16","author":"Berhe","year":"2024","journal-title":"Pharmaceutics"},{"key":"10.1016\/j.micpath.2026.108550_bib28","doi-asserted-by":"crossref","first-page":"194","DOI":"10.3389\/fcimb.2016.00194","article-title":"Antimicrobial peptides: an emerging category of therapeutic agents","volume":"6","author":"Mahlapuu","year":"2016","journal-title":"Front. Cell. Infect. Microbiol."},{"key":"10.1016\/j.micpath.2026.108550_bib29","doi-asserted-by":"crossref","first-page":"2226","DOI":"10.1039\/D1SC05662J","article-title":"Others, enhancing proline-rich antimicrobial peptide action by homodimerization: influence of bifunctional linker","volume":"13","author":"Li","year":"2022","journal-title":"Chem. Sci."},{"key":"10.1016\/j.micpath.2026.108550_bib30","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1097\/MOH.0b013e32831ac517","article-title":"The roles of cathelicidin LL-37 in immune defences and novel clinical applications","volume":"16","author":"Nijnik","year":"2009","journal-title":"Curr. Opin. Hematol."},{"key":"10.1016\/j.micpath.2026.108550_bib31","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1128\/CMR.00056-05","article-title":"Peptide antimicrobial agents","volume":"19","author":"Jenssen","year":"2006","journal-title":"Clin. Microbiol. Rev."},{"key":"10.1016\/j.micpath.2026.108550_bib32","doi-asserted-by":"crossref","first-page":"1321","DOI":"10.1016\/j.drudis.2016.06.018","article-title":"Self-assembly drug conjugates for anticancer treatment","volume":"21","author":"Fumagalli","year":"2016","journal-title":"Drug Discov. Today"},{"key":"10.1016\/j.micpath.2026.108550_bib33","doi-asserted-by":"crossref","DOI":"10.3389\/fchem.2019.00043","article-title":"Reassessing the host defense peptide landscape","volume":"7","author":"Haney","year":"2019","journal-title":"Front. Chem."},{"key":"10.1016\/j.micpath.2026.108550_bib34","doi-asserted-by":"crossref","first-page":"254","DOI":"10.1177\/0022034516679973","article-title":"Antimicrobial peptides: mechanisms of action and resistance","volume":"96","author":"Bechinger","year":"2017","journal-title":"J. Dent. Res."},{"key":"10.1016\/j.micpath.2026.108550_bib35","doi-asserted-by":"crossref","first-page":"6446","DOI":"10.1038\/s41598-018-24517-6","article-title":"Immunosilencing peptides by stereochemical inversion and sequence reversal: retro-d-peptides","volume":"8","author":"Arranz-Gibert","year":"2018","journal-title":"Sci. Rep."},{"key":"10.1016\/j.micpath.2026.108550_bib36","doi-asserted-by":"crossref","first-page":"4","DOI":"10.3390\/biom8010004","article-title":"Antimicrobial peptides: diversity, mechanism of action and strategies to improve the activity and biocompatibility in vivo","volume":"8","author":"Kumar","year":"2018","journal-title":"Biomolecules"},{"key":"10.1016\/j.micpath.2026.108550_bib37","doi-asserted-by":"crossref","first-page":"3547","DOI":"10.1016\/j.jmb.2018.12.015","article-title":"Peptide design principles for antimicrobial applications","volume":"431","author":"Torres","year":"2019","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.micpath.2026.108550_bib38","doi-asserted-by":"crossref","first-page":"3097","DOI":"10.3389\/fmicb.2019.03097","article-title":"Computer-aided design of antimicrobial peptides: are we generating effective drug candidates?","volume":"10","author":"Cardoso","year":"2020","journal-title":"Front. Microbiol."},{"key":"10.1016\/j.micpath.2026.108550_bib39","doi-asserted-by":"crossref","first-page":"482","DOI":"10.3390\/ijms22020482","article-title":"Therapeutic potential of antimicrobial peptides in polymicrobial biofilm-associated infections","volume":"22","author":"Batoni","year":"2021","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.micpath.2026.108550_bib40","doi-asserted-by":"crossref","first-page":"653","DOI":"10.1517\/14656566.7.6.653","article-title":"Antimicrobial peptides: therapeutic potential","volume":"7","author":"Zhang","year":"2006","journal-title":"Expert Opin. Pharmacother."}],"container-title":["Microbial Pathogenesis"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0882401026002767?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0882401026002767?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,7,11]],"date-time":"2026-07-11T06:40:18Z","timestamp":1783752018000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0882401026002767"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,8]]},"references-count":40,"alternative-id":["S0882401026002767"],"URL":"https:\/\/doi.org\/10.1016\/j.micpath.2026.108550","relation":{},"ISSN":["0882-4010"],"issn-type":[{"value":"0882-4010","type":"print"}],"subject":[],"published":{"date-parts":[[2026,8]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Rational engineering of a novel cationic LL-37\u2013temporin SHa hybrid peptide with anti-parasitic activity and effects on mitochondrial membrane potential in protozoan parasites","name":"articletitle","label":"Article Title"},{"value":"Microbial Pathogenesis","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.micpath.2026.108550","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2026 Elsevier Ltd. All rights are reserved, including those for text and data mining, AI training, and similar technologies.","name":"copyright","label":"Copyright"}],"article-number":"108550"}}