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Pesquisa do Estado de S?o Paulo","doi-asserted-by":"publisher","award":["2026\/02264-5"],"award-info":[{"award-number":["2026\/02264-5"]}],"id":[{"id":"10.13039\/501100001807","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002322","name":"Coordena??o de Aperfei?oamento de Pessoal de N?vel Superior","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100002322","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,9,29]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Recent research has demonstrated therapeutic potential against visceral leishmaniasis, a neglected disease with high prevalence and severity in very populated low- and middle-income regions; however, effective treatments for the cutaneous or mucocutaneous forms remain limited, despite their higher incidence. The negatively charged composition of Leishmania membranes differentiates it from the zwitterionic nature of mammalian cells, providing a basis for selective targeting by cationic peptides. Here, designed peptides (DecP-9, DecP-17, and DecP-18), spanning a broad range of charge and hydrophobicity, were evaluated and displayed distinct antileishmanial activity and selectivity, including effects on amastigote-infected macrophages. Biophysical studies revealed their interaction profiles: (i) DecP-9, with helical structure and strong lytic activity, showed high activity but low selectivity; (ii) DecP-18, enriched in \u03b2-stranded structures, exhibited limited partitioning, low lytic activity, and membrane translocation, resulting in low antiparasitic activity and high mammalian cell survival; (iii) DecP-17 displayed intermediate behavior, reducing intracellular amastigotes without significant cytotoxicity. Although there is a scenario of valued and challenging features in the development of therapeutic peptides, it seems that to find drug peptides that will cutaneously act, but whose ultimate target is the amastigote form contained inside the macrophage, a deeper understanding of membrane processes is required.<\/jats:p>","DOI":"10.1021\/acsomega.6c04342","type":"journal-article","created":{"date-parts":[[2026,9,16]],"date-time":"2026-09-16T05:02:05Z","timestamp":1789534925000},"page":"57046-57060","source":"Crossref","is-referenced-by-count":0,"title":["Assessing Designed\nModel Membrane-Targeting Peptides\nFound as Potential Molecular Scaffolds against Cutaneous Leishmaniasis"],"prefix":"10.1021","volume":"11","author":[{"given":"Viviane A. C.","family":"Santana","sequence":"first","affiliation":[{"name":"Universidade Estadual Paulista , , , ,","place":["Sa\u0303o Jose\u0301 do Rio Preto, SP, Brasil, 15054-000"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Danu\u0301bia B.","family":"Martins","sequence":"additional","affiliation":[{"name":"Universidade Estadual Paulista , , , ,","place":["Sa\u0303o Jose\u0301 do Rio Preto, SP, Brasil, 15054-000"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vanessa","family":"Albuquerque","sequence":"additional","affiliation":[{"name":"Instituto Butantan , , , ,","place":["Sa\u0303o Paulo, SP, Brasil, 05503-900"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anna Karoline","family":"Aguiar Fleuri Balbi","sequence":"additional","affiliation":[{"name":"Alimentos e Nutric\u0327a\u0303o - Universidade Federal do Mato Grosso do Sul , , , ,","place":["Campo Grande, MS, Brasil, 79070-900"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0009-0704-3592","authenticated-orcid":true,"given":"Jose\u0301 Eduardo","family":"Ferraz Souza","sequence":"additional","affiliation":[{"name":"Universidade Estadual Paulista , , , ,","place":["Sa\u0303o Jose\u0301 do Rio Preto, SP, Brasil, 15054-000"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2559-7344","authenticated-orcid":true,"given":"Andre Gustavo","family":"Tempone","sequence":"additional","affiliation":[{"name":"Instituto Butantan , , , ,","place":["Sa\u0303o Paulo, SP, Brasil, 05503-900"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marcelo","family":"Dias-Baruffi","sequence":"additional","affiliation":[{"name":"Universidade de Sa\u0303o Paulo , , , ,","place":["Ribeira\u0303o Preto, SP, Brasil, 14040-903"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thalita","family":"Riul","sequence":"additional","affiliation":[{"name":"Alimentos e Nutric\u0327a\u0303o - Universidade Federal do Mato Grosso do Sul , , , ,","place":["Campo Grande, MS, Brasil, 79070-900"]},{"name":"Universidade de Sa\u0303o Paulo , , , ,","place":["Ribeira\u0303o Preto, SP, Brasil, 14040-903"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6521-9148","authenticated-orcid":true,"given":"Dayane S.","family":"Alvares","sequence":"additional","affiliation":[{"name":"Universidade Estadual Paulista , , , ,","place":["Sa\u0303o Jose\u0301 do Rio Preto, SP, Brasil, 15054-000"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7443-2883","authenticated-orcid":true,"given":"Marcia Perez","family":"dos Santos Cabrera","sequence":"additional","affiliation":[{"name":"Universidade Estadual Paulista , , , ,","place":["Sa\u0303o Jose\u0301 do Rio Preto, SP, Brasil, 15054-000"]},{"name":"Universidade Estadual Paulista , , , ,","place":["Sa\u0303o Jose\u0301 do Rio Preto, SP, Brasil, 15054-000"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2026,9,16]]},"reference":[{"key":"2026092911125233800_cit1","doi-asserted-by":"publisher","first-page":"74","DOI":"10.1038\/s41392-024-02107-5","article-title":"Advance in peptide-based\ndrug development: delivery platforms, therapeutics and vaccines","volume":"10","author":"Xiao","year":"2025","journal-title":"Signal Transduction Targeted Ther."},{"issue":"9","key":"2026092911125233800_cit2","doi-asserted-by":"publisher","first-page":"4400","DOI":"10.3390\/ijms22094400","article-title":"Peptides to tackle Leishmaniasis:\ncurrent status and future directions","volume":"22","author":"Robles-Loaiza","year":"2021","journal-title":"Int. J.\nMol. Sci."},{"issue":"8","key":"2026092911125233800_cit3","doi-asserted-by":"publisher","first-page":"2467","DOI":"10.1021\/acsinfecdis.4c00089","article-title":"Targeting Leishmania promastigotes and amastigotes forms through amino\nacids and peptides: a promising therapeutic strategy","volume":"10","author":"Registre","year":"2024","journal-title":"ACS Infect. Dis."},{"issue":"8","key":"2026092911125233800_cit4","first-page":"868","article-title":"Antimicrobial peptides for leishmaniasis","volume":"11","author":"Cobb","year":"2010","journal-title":"Curr. Opin. Invest. Drugs"},{"issue":"2","key":"2026092911125233800_cit5","doi-asserted-by":"publisher","first-page":"122","DOI":"10.1007\/s00436-024-08133-0","article-title":"Therapeutic\npotential of antimicrobial\npeptides against pathogenic protozoa","volume":"123","author":"Hagemann","year":"2024","journal-title":"Parasitol.\nRes."},{"key":"2026092911125233800_cit6","doi-asserted-by":"publisher","first-page":"35","DOI":"10.1038\/s41579-022-00777-y","article-title":"Anti-trypanosomatid\ndrug discovery: progress and challenges","volume":"21","author":"De Rycker","year":"2023","journal-title":"Nat.\nRev. Microbiol."},{"issue":"10","key":"2026092911125233800_cit7","doi-asserted-by":"publisher","first-page":"563","DOI":"10.3390\/toxins11100563","article-title":"Natural occurrence in venomous arthropods of antimicrobial\npeptides active against protozoan parasites","volume":"11","author":"Sabia\u0301 Ju\u0301nior","year":"2019","journal-title":"Toxins"},{"issue":"9","key":"2026092911125233800_cit8","doi-asserted-by":"publisher","first-page":"1047","DOI":"10.2217\/fmb.12.85","article-title":"Modes of\naction of Leishmanicidal\nantimicrobial peptides","volume":"7","author":"Marr","year":"2012","journal-title":"Future Microbiol."},{"issue":"9","key":"2026092911125233800_cit9","doi-asserted-by":"publisher","first-page":"1138","DOI":"10.2174\/138945012802002393","article-title":"Antimicrobial peptide\naction on parasites","volume":"13","author":"Torrent","year":"2012","journal-title":"Curr. Drug Targets"},{"issue":"22","key":"2026092911125233800_cit10","doi-asserted-by":"publisher","first-page":"6474","DOI":"10.1111\/j.1742-4658.2009.07358.x","article-title":"Multifunctional\nhost defense peptides: antiparasitic activities","volume":"276","author":"Mor","year":"2009","journal-title":"FEBS J."},{"issue":"6","key":"2026092911125233800_cit11","doi-asserted-by":"publisher","first-page":"649","DOI":"10.2174\/1566524043360069","article-title":"Surface determinants of Leishmania\nparasites and their role in infectivity in the mammalian host","volume":"4","author":"Naderer","year":"2004","journal-title":"Curr. Mol. Med."},{"issue":"11","key":"2026092911125233800_cit12","doi-asserted-by":"publisher","first-page":"2861","DOI":"10.1016\/j.bbagen.2017.08.003","article-title":"Membrane\ntargeting peptides toward antileishmanial activity: design, structural\ndetermination and mechanism of interaction","volume":"1861","author":"Martins","year":"2017","journal-title":"Biochim. Biophys. Acta"},{"key":"2026092911125233800_cit13","doi-asserted-by":"publisher","first-page":"501","DOI":"10.1111\/cbdd.12970","article-title":"MD simulations\nand multivariate studies for modeling the antileishmanial activity\nof peptides","volume":"90","author":"Guerra","year":"2017","journal-title":"Chem. Biol. Drug Des."},{"issue":"12","key":"2026092911125233800_cit14","doi-asserted-by":"publisher","first-page":"2320","DOI":"10.1016\/j.peptides.2007.09.017","article-title":"Decoralin, a novel linear cationic alpha-helical peptide\nfrom the venom of the solitary eumenine wasp Oreumenes decoratus","volume":"28","author":"Konno","year":"2007","journal-title":"Peptides"},{"issue":"13","key":"2026092911125233800_cit15","doi-asserted-by":"publisher","first-page":"4266","DOI":"10.1021\/bi052150y","article-title":"Effect of\nnatural l- to d-amino acid\nconversion on the organization, membrane binding, and biological function\nof the antimicrobial peptides Bombinins H","volume":"45","author":"Mangoni","year":"2006","journal-title":"Biochemistry"},{"issue":"2","key":"2026092911125233800_cit16","doi-asserted-by":"publisher","first-page":"123","DOI":"10.1007\/s00436-002-0728-y","article-title":"Biochemical analysis\nof proteins and lipids found in parasitophorous vacuoles containing\nLeishmania amazonensis","volume":"89","author":"Henriques","year":"2003","journal-title":"Parasitol. Res."},{"issue":"1\u20132","key":"2026092911125233800_cit17","doi-asserted-by":"publisher","first-page":"141","DOI":"10.1016\/S0005-2736(99)00204-7","article-title":"Differential scanning\ncalorimetry and X-ray diffraction\nstudies of the specificity of the interaction of antimicrobial peptides\nwith membrane-mimetic systems","volume":"1462","author":"Lohner","year":"1999","journal-title":"Biochim. Biophys.\nActa Gen. Subj."},{"key":"2026092911125233800_cit18","doi-asserted-by":"publisher","first-page":"428","DOI":"10.1134\/S0022093011050045","article-title":"Lipid composition\nof cells and low-density lipoproteins in blood serum of human and\nsome vertebrate species","volume":"47","author":"Lizenko","year":"2011","journal-title":"J. Evol. Biochem. Physiol."},{"issue":"6","key":"2026092911125233800_cit19","doi-asserted-by":"publisher","first-page":"1817","DOI":"10.1096\/fj.07-096081","article-title":"Human antimicrobial\npeptide histatin 5 is a cell-penetrating peptide targeting mitochondrial\nATP synthesis in Leishmania","volume":"22","author":"Luque-Ortega","year":"2008","journal-title":"FASEB J."},{"issue":"9","key":"2026092911125233800_cit20","doi-asserted-by":"publisher","first-page":"3855","DOI":"10.1128\/AAC.00548-09","article-title":"In vitro susceptibilities\nof Leishmania donovani promastigote and amastigote\nstages to antileishmanial reference\ndrugs: practical relevance of stage-specific differences","volume":"53","author":"Vermeersch","year":"2009","journal-title":"Antimicrob. Agents Chemother."},{"issue":"1","key":"2026092911125233800_cit21","doi-asserted-by":"publisher","first-page":"11","DOI":"10.1016\/j.exppara.2009.05.002","article-title":"Antiplasmodial and antileishmanial activities of phylloseptin-1,\nan antimicrobial peptide from the skin secretion of Phyllomedusa azurea\n(Amphibia)","volume":"123","author":"Ku\u0308ckelhaus","year":"2009","journal-title":"Exp. Parasitol."},{"issue":"4","key":"2026092911125233800_cit22","doi-asserted-by":"publisher","first-page":"565","DOI":"10.1016\/j.peptides.2004.11.002","article-title":"a novel class\nof anti-bacterial and\nanti-protozoan peptides from the Phyllomedusa genus","volume":"26","author":"Leite","year":"2005","journal-title":"Peptides"},{"issue":"2","key":"2026092911125233800_cit23","doi-asserted-by":"publisher","first-page":"361","DOI":"10.1042\/bj3560361","article-title":"Effects\nof histatin 5 and derived peptides on Candida albicans","volume":"356","author":"Ruissen","year":"2001","journal-title":"Biochem. J."},{"issue":"3","key":"2026092911125233800_cit24","doi-asserted-by":"publisher","first-page":"665","DOI":"10.1042\/BJ20031785","article-title":"Interactions of histatin 5 and histatin 5-derived peptides\nwith liposome membranes: surface effects, translocation and permeabilization","volume":"379","author":"Den Hertog","year":"2004","journal-title":"Biochem. J."},{"issue":"13","key":"2026092911125233800_cit25","doi-asserted-by":"publisher","first-page":"6412","DOI":"10.1021\/am401629p","article-title":"Immobilization studies\nof an engineered arginine-tryptophan-rich peptide on a silicone surface\nwith antimicrobial and antibiofilm activity","volume":"5","author":"Lim","year":"2013","journal-title":"ACS Appl. Mater. Interfaces"},{"issue":"1","key":"2026092911125233800_cit26","doi-asserted-by":"publisher","first-page":"125","DOI":"10.1016\/0022-2836(84)90309-7","article-title":"Analysis of membrane\nand surface protein sequences with the hydrophobic moment plot","volume":"179","author":"Eisenberg","year":"1984","journal-title":"J. Mol. Biol."},{"key":"2026092911125233800_cit27","doi-asserted-by":"publisher","first-page":"2101","DOI":"10.1093\/bioinformatics\/btn392","article-title":"HELIQUEST:\na web server\nto screen sequences with specific \u03b1-helical properties","volume":"24","author":"Gautier","year":"2008","journal-title":"Bioinformatics"},{"issue":"7","key":"2026092911125233800_cit28","doi-asserted-by":"publisher","first-page":"670","DOI":"10.3390\/membranes13070670","article-title":"Triggering the amphotericin B pore-forming\nactivity by phytochemicals","volume":"13","author":"Efimova","year":"2023","journal-title":"Membranes"},{"issue":"2","key":"2026092911125233800_cit29","doi-asserted-by":"publisher","first-page":"194","DOI":"10.1021\/bi501392n","article-title":"Translocation mechanism(s) of cell-penetrating\npeptides: biophysical studies using artificial membrane bilayers","volume":"54","author":"Di Pisa","year":"2015","journal-title":"Biochemistry"},{"issue":"4","key":"2026092911125233800_cit30","doi-asserted-by":"publisher","first-page":"2484","DOI":"10.1128\/AAC.02328-15","article-title":"Identification of synthetic and natural\nhost defense peptides with leishmanicidal activity","volume":"60","author":"Marr","year":"2016","journal-title":"Antimicrob. Agents Chemother."},{"issue":"9","key":"2026092911125233800_cit31","doi-asserted-by":"publisher","first-page":"1060","DOI":"10.1007\/s00018-005-5536-y","article-title":"Temporins,\nanti-infective peptides with expanding properties","volume":"63","author":"Mangoni","year":"2006","journal-title":"Cell. Mol. Life Sci."},{"key":"2026092911125233800_cit32","doi-asserted-by":"publisher","first-page":"603","DOI":"10.1002\/psc.853","article-title":"Biological characterization\nand modes\nof action of temporins and Bombinins H, multiple forms of short and\nmildly cationic anti-microbial peptides from amphibian skin","volume":"13","author":"Mangoni","year":"2007","journal-title":"J. Peptide Sci."},{"issue":"2","key":"2026092911125233800_cit33","doi-asserted-by":"publisher","first-page":"2775","DOI":"10.3390\/molecules20022775","article-title":"The role of phosphoglycans\nin the susceptibility of\nLeishmania mexicana to the temporin family of anti-microbial peptides","volume":"20","author":"Eggimann","year":"2015","journal-title":"Molecules"},{"key":"2026092911125233800_cit34","doi-asserted-by":"publisher","first-page":"605","DOI":"10.1007\/s12551-025-01312-y","article-title":"Unlocking the power of membrane biophysics:\nenhancing\nthe study of antimicrobial peptides activity and selectivity","volume":"17","author":"Bertrand","year":"2025","journal-title":"Biophys. Rev."},{"issue":"5","key":"2026092911125233800_cit35","doi-asserted-by":"publisher","first-page":"936","DOI":"10.1016\/j.bpj.2015.07.033","article-title":"PE and\nPS lipids synergistically enhance membrane poration\nby a peptide with anticancer properties","volume":"109","author":"Leite","year":"2015","journal-title":"Biophys.\nJ."},{"issue":"34","key":"2026092911125233800_cit36","doi-asserted-by":"publisher","first-page":"11045","DOI":"10.1021\/bi036054d","article-title":"Vesicle Membrane\nInteractions of Penetratin Analogues","volume":"43","author":"Persson","year":"2004","journal-title":"Biochemistry"},{"issue":"Web Server","key":"2026092911125233800_cit37","doi-asserted-by":"publisher","first-page":"W668","DOI":"10.1093\/nar\/gkh371","article-title":"DICHROWEB, an online\nserver for protein secondary structure\nanalyses from circular dichroism spectroscopic data","volume":"32","author":"Whitmore","year":"2004","journal-title":"Nucleic Acids Res."},{"issue":"4","key":"2026092911125233800_cit38","doi-asserted-by":"publisher","first-page":"481","DOI":"10.1007\/s00249-010-0661-4","article-title":"Using zeta-potential measurements\nto quantify peptide partition to lipid membranes","volume":"40","author":"Freire","year":"2011","journal-title":"Eur. Biophys. J."},{"key":"2026092911125233800_cit39","doi-asserted-by":"publisher","first-page":"91","DOI":"10.1007\/s00726-010-0511-9","article-title":"The effect\nof acidic residues and amphipathicity on the lytic activities of mastoparan\npeptides studied by fluorescence and CD spectroscopy","volume":"40","author":"Leite","year":"2011","journal-title":"Amino Acids"},{"key":"2026092911125233800_cit40","doi-asserted-by":"publisher","first-page":"546","DOI":"10.1002\/cbic.200600553","article-title":"A simple fluorescence-spectroscopic\nmembrane translocation assay","volume":"8","author":"Keller","year":"2007","journal-title":"ChemBioChem"},{"issue":"3","key":"2026092911125233800_cit41","doi-asserted-by":"publisher","first-page":"449","DOI":"10.3390\/biom15030449","article-title":"Enhancing antimicrobial\npeptides from frog skin: a rational approach","volume":"15","author":"Aguilar","year":"2025","journal-title":"Biomolecules"},{"key":"2026092911125233800_cit42","doi-asserted-by":"publisher","first-page":"353","DOI":"10.1007\/978-0-387-46312-4","volume-title":"Principles of fluorescence\nspectroscopy","author":"Lakowicz","year":"2006","edition":"3"},{"issue":"5","key":"2026092911125233800_cit43","doi-asserted-by":"publisher","first-page":"1815","DOI":"10.1016\/j.bpj.2008.11.053","article-title":"Synergistic effects of the membrane\nactions of cecropin-melittin antimicrobial hybrid peptide BP100","volume":"96","author":"Ferre","year":"2009","journal-title":"Biophys. J."},{"key":"2026092911125233800_cit44","doi-asserted-by":"publisher","first-page":"271","DOI":"10.1007\/978-1-60761-447-0_19","article-title":"Membrane translocation assayed by\nfluorescence spectroscopy","volume":"606","author":"Broecker","year":"2010","journal-title":"Methods Mol. Biol."},{"key":"2026092911125233800_cit45","doi-asserted-by":"publisher","first-page":"2281","DOI":"10.1007\/s00018-011-0719-1","article-title":"Fluorescence spectroscopy and molecular\ndynamics simulations\nin studies on the mechanism of membrane destabilization by antimicrobial\npeptides","volume":"68","author":"Bocchinfuso","year":"2011","journal-title":"Cell. Mol. Life Sci."},{"issue":"22","key":"2026092911125233800_cit46","doi-asserted-by":"publisher","first-page":"6483","DOI":"10.1111\/j.1742-4658.2009.07359.x","article-title":"Multifunctional\nhost defense peptides: intracellular-targeting antimicrobial peptides","volume":"276","author":"Nicolas","year":"2009","journal-title":"FEBS J."},{"key":"2026092911125233800_cit47","doi-asserted-by":"publisher","first-page":"74","DOI":"10.1016\/j.abb.2018.11.010","article-title":"1988\u20132018:\nThirty years of\ndrug smuggling at the nanoscale. Challenges and opportunities of cell-penetrating\npeptides in biomedical research","volume":"661","author":"Gallo","year":"2019","journal-title":"Arch. 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