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(Referência obtida automaticamente do Web of Science, por meio da informação sobre o financiamento pela FAPESP e o número do processo correspondente, incluída na publicação pelos autores.)

Comparative study of the mechanism of action of the antimicrobial peptide gomesin and its linear analogue: The role of the beta-hairpin structure

Texto completo
Autor(es):
Domingues, Tatiana M. [1] ; Perez, Katia R. [1] ; Miranda, Antonio [1] ; Riske, Karin A. [1]
Número total de Autores: 4
Afiliação do(s) autor(es):
[1] Univ Fed Sao Paulo, Escola Paulista Med, Dept Biofis, BR-04039032 Sao Paulo, SP - Brazil
Número total de Afiliações: 1
Tipo de documento: Artigo Científico
Fonte: BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES; v. 1848, n. 10, A, p. 2414-2421, OCT 2015.
Citações Web of Science: 8
Resumo

Gomesin (Gm) is an antimicrobial peptide first isolated from the hemolymph of a Brazilian spider. Its powerful antimicrobial activity is, however, accompanied by hemolysis. As an alternative to this issue, a linear analogue (named GmL) lacking the disulfide bonds was designed. Here, CD spectroscopy, a fluorescence-based leakage assay, isothermal titration calorimety (ITC) and light scattering are used to study the interaction of both Gm and GmL with large unilamellar vesicles (LUVs) composed of POPC (palmitoyl oleoyl phosphatidylcholine) with 25 and 50 mol% POPG (palmitoyl oleoyl phosphatidylglycerol). The activities of Gm and GmL in respect to their binding affinity/enthalpy, ability to permeabilize membranes and to induce vesicle aggregation are correlated with peptide secondary structure. Whereas Gm displays a quite stable beta-hairpin motif irrespective of the environment, GmL assumes a random conformation in aqueous solution and in the presence of 25 mol% POPG but adopts a beta-like structure in the presence of 50 mol% POPG. Gm exhibited high lyric activity against both surface charge densities. Instead, the activity of GmL was found to be negligible in the presence of 25 mol% POPG LUVs, but comparable to that of the native peptide against 50 mol% POPG as a consequence of peptide structuring. We conclude that the activity of Gm and its linear analogue is intimately related to the formation of a beta-turn motif, in which the hydrophobic residues form a hydrophobic face able to insert into the membrane and disrupt it. (c) 2015 Elsevier B.V. All rights reserved. (AU)

Processo FAPESP: 12/10442-8 - Perturbações em bicamadas lipídicas carregadas induzidas por pulsos elétricos, peptídeos antimicrobianos e vesículas de carga oposta
Beneficiário:Karin Do Amaral Riske
Linha de fomento: Auxílio à Pesquisa - Regular
Processo FAPESP: 09/54558-7 - Estudos de sintese, conformacao e atividade biologica da gomesina e analogos atraves de diferentes metodologias.
Beneficiário:Tatiana Moreira Domingues
Linha de fomento: Bolsas no Brasil - Doutorado
Processo FAPESP: 08/57685-7 - Instituto Nacional de Ciência e Tecnologia de Fluídos Complexos
Beneficiário:Antonio Martins Figueiredo Neto
Linha de fomento: Auxílio à Pesquisa - Temático