Please use this identifier to cite or link to this item: https://repositorio.unifesp.br/handle/11600/58124
Title: Biophysical and biological properties of small linear peptides derived from crotamine, a cationic antimicrobial/antitumoral toxin with cell penetrating and cargo delivery abilities
Authors: Dal Mas, C. [UNIFESP]
Pinheiro, D. A. [UNIFESP]
Campeiro, J. D. [UNIFESP]
Mattei, B. [UNIFESP]
Oliveira, V. [UNIFESP]
Oliveira, E. B.
Miranda, A. [UNIFESP]
Perez, K. R. [UNIFESP]
Hayashi, M. A. F. [UNIFESP]
Keywords: Crotalus durissus terrificus
Venom
Crotamine
Linear cationic peptide
Antifungal
Snake toxin
Issue Date: 2017
Publisher: Elsevier Science Bv
Citation: Biochimica Et Biophysica Acta-Biomembranes. Amsterdam, v. 1859, n. 12, p. 2340-2349, 2017.
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.
URI: https://repositorio.unifesp.br/handle/11600/58124
ISSN: 0005-2736
Other Identifiers: http://dx.doi.org/10.1016/j.bbamem.2017.09.006
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