The conformation of fusogenic B18 peptide in surfactant solutions

• Type: Article in International Scientific Journal
• Date: 2008

Authors

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

Journal

Title: Journal of Peptide Science

Vol. 14 No. 8

Pages: 436-441

ISSN: 1075-2617

Publisher: Wiley-Blackwell

Indexing

ISI Web of Knowledge - 10 Citations

ISI Web of Science

Scopus - 9 Citations

Scientific classification

FOS: Natural sciences > Chemical sciences

CORDIS: Health sciences

Other information

Authenticus ID: 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.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 6