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

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

Author Dal Mas, C. Autor UNIFESP Google Scholar
Pinheiro, D. A. Autor UNIFESP Google Scholar
Campeiro, J. D. Autor UNIFESP Google Scholar
Mattei, B. Autor UNIFESP Google Scholar
Oliveira, V. Autor UNIFESP Google Scholar
Oliveira, E. B. Google Scholar
Miranda, A. Autor UNIFESP Google Scholar
Perez, K. R. Autor UNIFESP Google Scholar
Hayashi, M. A. F. Autor UNIFESP Google Scholar
Abstract Crotamine 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.
Keywords Crotalus durissus terrificus
Venom
Crotamine
Linear cationic peptide
Antifungal
Snake toxin
xmlui.dri2xhtml.METS-1.0.item-coverage Amsterdam
Language English
Sponsor Fundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP)
Conselho Nacional de Desenvolvimento Cientifico e Tecnologico (CNPq)
Grant number FAPESP: 2013/13392-4
FAPESP: 2017/02413-1
CNPq: 311815/2012-0
CNPq: 475739/2013-2
CNPq: 39337/2016-0
Date 2017
Published in Biochimica Et Biophysica Acta-Biomembranes. Amsterdam, v. 1859, n. 12, p. 2340-2349, 2017.
ISSN 0005-2736 (Sherpa/Romeo, impact factor)
Publisher Elsevier Science Bv
Extent 2340-2349
Origin http://dx.doi.org/10.1016/j.bbamem.2017.09.006
Access rights Open access Open Access
Type Article
Web of Science ID WOS:000415770900007
URI https://repositorio.unifesp.br/handle/11600/58124

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