The conformation of fusogenic B18 peptide in surfactant solutions

• Tipo: Artigo em Revista Científica Internacional
• Data: 2008

Autores

Sandra Rocha (Autor) Outra; Marlene Lucio (Autor) FFUP; Carmo C Pereira (Autor) FEUP; Saletre Reis (Autor) FFUP; Gerald Brezesinski (Autor) Outra

Revista

Título: Journal of Peptide Science

Vol. 14 Nº 8

Páginas: 436-441

ISSN: 1075-2617

Editora: Wiley-Blackwell

Indexação

ISI Web of Knowledge - 10 Citações

ISI Web of Science

Scopus - 9 Citações

Classificação Científica

FOS: Ciências exactas e naturais > Química

CORDIS: Ciências da Saúde

Outras Informações

ID Authenticus: P-004-0KW

DOI: 10.1002/pse.935

Resumo (PT): The interaction of B18 peptide with surfactants has been studied by circular dichroism spectroscopy and fluorescence measurements. B18 is the fusogenic motif of the fertilization sea urchin protein. The peptide forms an -helix structure when interacting with positively or negatively charged surfactants below and above the critical micellar concentration (CMC). The -helix formation is due to binding of surfactant monomers rather than the formation of surfactant micelles on the peptide. Fluorescence measurements show that the CMC of the negatively charged surfactant increases in the presence of B18, supporting the fact that there is a strong interaction between the peptide and monomers. Nonionic surfactant monomers have no effect on the peptide structure, whereas the micelles induce an -helical conformation. In this case the helix stabilization results from the formation of surfactant micelles on the peptide <br> <br> Keywords conformational analysis • B18 peptide • charged and nonionic surfactants • circular dichroism • fluorescence measurements <br> <a target="_blank" href="http://www3.interscience.wiley.com/journal/116840945/abstract"> Texto integral </a> <br> <br>

Abstract (EN): The interaction of B18 peptide with surfactants has been studied by circular dichroism spectroscopy and fluorescence measurements. B18 is the fusogenic motif of the fertilization sea urchin protein. The peptide forms an a-helix structure when interacting with positively or negatively charged surfactants below and above the critical micellar concentration (CMC). The a-helix formation is due to binding of surfactant monomers rather than the formation of surfactant micelles on the peptide. Fluorescence measurements show that the CMC of the negatively charged surfactant increases in the presence of B IS, supporting the fact that there is a strong interaction between the peptide and monomers. Nonionic surfactant monomers have no effect on the peptide structure, whereas the micelles induce an a-helical conformation. In this case the helix stabilization results from the formation of surfactant micelles on the peptide. Copyright (c) 2007 European Peptide Society and John Wiley & Sons, Ltd.

Idioma: Inglês

Tipo (Avaliação Docente): Científica

Nº de páginas: 6