Biophysical and biological properties of small linear peptides derived from crotamine, a cationic antimicrobial/antitumoral toxin with cell penetrating and cargo delivery abilities

dc.citation.issue12
dc.citation.volume1859
dc.contributor.authorDal Mas, C. [UNIFESP]
dc.contributor.authorPinheiro, D. A. [UNIFESP]
dc.contributor.authorCampeiro, J. D. [UNIFESP]
dc.contributor.authorMattei, B. [UNIFESP]
dc.contributor.authorOliveira, V. [UNIFESP]
dc.contributor.authorOliveira, E. B.
dc.contributor.authorMiranda, A. [UNIFESP]
dc.contributor.authorPerez, K. R. [UNIFESP]
dc.contributor.authorHayashi, M. A. F. [UNIFESP]
dc.coverageAmsterdam
dc.date.accessioned2020-09-01T13:21:12Z
dc.date.available2020-09-01T13:21:12Z
dc.date.issued2017
dc.description.abstractCrotamine is a natural polypeptide from snake venom which delivers nucleic acid molecules into cells, besides having pronounced affinity for negatively charged membranes and antifungal activity. We previously demonstrated that crotamine derived short linear peptides were not very effective as antifungal, although the non structured recombinant crotamine was overridingly more potent compared to the native structured crotamine. Aiming to identify the features necessary for the antifungal activity of crotamine, two linear short peptides, each comprising half of the total positively charged amino acid residues of the full-length crotamine were evaluated here to show that these linear peptides keep the ability to interact with lipid membrane model systems with different phospholipid compositions, even after forming complexes with DNA. Interestingly, the presence of cysteine residues in the structure of these linear peptides highly influenced the antifungal activity, which was not associated to the lipid membrane lytic activity. In addition to the importance of the positive charges, the crucial role of cysteine residues was noticed for these linear analogs of crotamine, although the tridimensional structure and lipid membrane lytic activity observed only for native crotamine was not essential for the antifungal activity. As these peptides still keep the ability to form complexes with DNA molecules with no prejudice to their ability to bind to lipid membranes, they may be potentially advantageous as membrane translocation vector, as they do not show lipid membrane lytic activity and may harbor or not antifungal activity, by keeping or not the semi-essential amino acid cysteine in their sequence.en
dc.description.affiliationUniv Fed Sao Paulo UNIFESP EPM, Dept Farmacol, Sao Paulo, Brazil
dc.description.affiliationUniv Fed Sao Paulo UNIFESP EPM, Dept Biofis, Sao Paulo, Brazil
dc.description.affiliationUniv Sao Paulo USP RP, Dept Bioquim & Imunol, Ribeirao Preto, Brazil
dc.description.affiliationUnifespUniv Fed Sao Paulo UNIFESP EPM, Dept Farmacol, Sao Paulo, Brazil
dc.description.affiliationUnifespUniv Fed Sao Paulo UNIFESP EPM, Dept Biofis, Sao Paulo, Brazil
dc.description.sourceWeb of Science
dc.description.sponsorshipFundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Cientifico e Tecnologico (CNPq)
dc.description.sponsorshipIDFAPESP: 2013/13392-4
dc.description.sponsorshipIDFAPESP: 2017/02413-1
dc.description.sponsorshipIDCNPq: 311815/2012-0
dc.description.sponsorshipIDCNPq: 475739/2013-2
dc.description.sponsorshipIDCNPq: 39337/2016-0
dc.format.extent2340-2349
dc.identifierhttp://dx.doi.org/10.1016/j.bbamem.2017.09.006
dc.identifier.citationBiochimica Et Biophysica Acta-Biomembranes. Amsterdam, v. 1859, n. 12, p. 2340-2349, 2017.
dc.identifier.doi10.1016/j.bbamem.2017.09.006
dc.identifier.issn0005-2736
dc.identifier.urihttps://repositorio.unifesp.br/handle/11600/58124
dc.identifier.wosWOS:000415770900007
dc.language.isoeng
dc.publisherElsevier Science Bv
dc.relation.ispartofBiochimica Et Biophysica Acta-Biomembranes
dc.rightsAcesso aberto
dc.subjectCrotalus durissus terrificusen
dc.subjectVenomen
dc.subjectCrotamineen
dc.subjectLinear cationic peptideen
dc.subjectAntifungalen
dc.subjectSnake toxinen
dc.titleBiophysical and biological properties of small linear peptides derived from crotamine, a cationic antimicrobial/antitumoral toxin with cell penetrating and cargo delivery abilitiesen
dc.typeArtigo
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