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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.)

Effect of the aspartic acid D2 on the affinity of Polybia-MP1 to anionic lipid vesicles

Texto completo
Autor(es):
Leite, Natalia Bueno [1] ; Alvares, Dayane dos Santos [1] ; de Souza, Bibiana Monson [2] ; Palma, Mario Sergio [2] ; Ruggiero Neto, Joao [1]
Número total de Autores: 5
Afiliação do(s) autor(es):
[1] UNESP, Sao Paulo State Univ, IBILCE, Dept Phys, Sao Jose Do Rio Preto, SP - Brazil
[2] UNESP, Sao Paulo State Univ, Ctr Studies Social Insects, Dept Biol, IB, Rio Claro, SP - Brazil
Número total de Afiliações: 2
Tipo de documento: Artigo Científico
Fonte: EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS; v. 43, n. 4-5, p. 121-130, MAY 2014.
Citações Web of Science: 6
Resumo

Polybia-MP1 (IDWKKLLDAAKQIL-NH2), a helical peptide extracted from the venom of a Brazilian wasp, has broad-spectrum antimicrobial activities without being hemolytic or cytotoxic. This peptide has also displayed anticancer activity against cancer cell cultures. Despite its high selectivity, MP1 has an unusual low net charge (Q = +2). The aspartic residue (D2) in the N-terminal region plays an important role in its affinity and selectivity; its substitution by asparagine (D2N mutant) led to a less selective peptide. Aiming to explore the importance of this residue for the peptides' affinity, we compared the zwitterionic and anionic vesicle adsorption activity of Polybia-MP1 versus its D2N mutant and also mastoparan X (MPX). The adsorption, electrostatic, and conformational free energies were assessed by circular dichroism (CD) and fluorescence titrations using large unilamellar vesicles (LUVs) at the same conditions in association with measurement of the zeta potential of LUVs in the presence of the peptides. The adsorption free energies of the peptides, determined from the partition coefficients, indicated higher affinity of MP1 to anionic vesicles compared with the D2N mutant and MPX. The electrostatic and conformational free energies of MP1 in anionic vesicles are less favorable than those found for the D2N mutant and MPX. Therefore, the highest affinity of MP1 to anionic vesicles is likely due to other energetic contributions. The presence of D2 in MP1 makes these energetic components 1.2 and 1.5 kcal/mol more favorable compared with the D2N mutant and MPX, respectively. (AU)

Processo FAPESP: 12/08147-8 - Estudo da formação de domínios em membranas modelo induzidos por peptídeos antimicrobianos e sua ação interfacial
Beneficiário:Dayane dos Santos Alvares
Linha de fomento: Bolsas no Brasil - Doutorado
Processo FAPESP: 11/11640-5 - Interação de peptídeos líticos e membranas modelo: ação interfacial e indução de domínios lipídicos
Beneficiário:João Ruggiero Neto
Linha de fomento: Auxílio à Pesquisa - Regular