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Title: Conformational and functional studies of gomesin analogues by CD, EPR and fluorescence spectroscopies
Authors: Moraes, Luis Guilherme Mello [UNIFESP]
Fázio, Marcos Antonio [UNIFESP]
Vieira, Renata de Freitas Fischer
Nakaie, Clovis Ryuichi
Miranda, Maria Teresa Machini
Schreier, Shirley
Daffre, Sirlei
Miranda, Antonio [UNIFESP]
Universidade Federal de São Paulo (UNIFESP)
Universidade de São Paulo (USP)
Keywords: gomesin
antimicrobial peptide
solid-phase peptide synthesis
electron paramagnetic resonance
circular dichroism
Issue Date: 1-Jan-2007
Publisher: Elsevier B.V.
Citation: Biochimica Et Biophysica Acta-biomembranes. Amsterdam: Elsevier B.V., v. 1768, n. 1, p. 52-58, 2007.
Abstract: The aim of this work was to examine the bioactivity and the conformational behavior of some gomesin (Gm) analogues in different environments that mimic the biological membrane/water interface. Thus, manual peptide synthesis was performed by the solid-phase method, antimicrobial activity was evaluated by a liquid growth inhibition assay, and conformational studies were performed making use of several spectroscopic techniques: CD, fluorescence and EPR. [TOAC(1)]-Gm; [TOAC(1), Ser(2,6,11,15)]-Gm; [Trp(7)]-Gm; [Ser(2,6,11,15), Trp(7)]-Gm; [Trp(9)]-Gm; and [Ser(2,6,11,15), Trp(9)]-Gm were synthesized and tested. the results indicated that incorporation of TOAC or Trp caused no significant reduction of antimicrobial activity; the cyclic analogues presented a beta-hairpin conformation similar to that of Gm. All analogues interacted with negatively charged SDS both above and below the detergent's critical micellar concentration (cmc). in contrast, while Gm and [TOAC(1)]-Gm required higher LPC concentrations to bind to micelles of this zwitterionic detergent, the cyclic Trp derivatives and the linear derivatives did not seem to interact with this membrane-mimetic system. These data corroborate previous results that suggest that electrostatic interactions with the lipid bilayer of microorganisms play an important role in the mechanism of action of gomesin. Moreover, the results show that hydrophobic interactions also contribute to membrane binding of this antimicrobial peptide. (c) 2006 Elsevier B.V. All rights reserved.
ISSN: 0005-2736
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