Headgroup specificity for the interaction of the antimicrobial peptide tritrpticin with phospholipid Langmuir monolayers

Headgroup specificity for the interaction of the antimicrobial peptide tritrpticin with phospholipid Langmuir monolayers

Author Salay, Luiz C. Google Scholar
Ferreira, Marystela Google Scholar
Oliveira, Osvaldo N. Google Scholar
Nakaie, Clovis R. Autor UNIFESP Google Scholar
Schreier, Shirley Google Scholar
Institution Universidade de São Paulo (USP)
Universidade Federal de São Carlos (UFSCar)
Universidade Federal de São Paulo (UNIFESP)
Abstract We examined the interaction of the cationic antimicrobial peptide (AMP) tritrpticin (VRRFPWWWPFLRR, TRP3) with Langmuir monolayers of zwitterionic (dipalmitoyl phosphatidylcholine, DPPC, and dipalmitoyl phosphatidylethanolamine, DPPE) and negatively charged phospholipids (dipalmitoyl phosphatidic acid, DPPA, and dipalmitoyl phosphatidylglycerol, DPPG). Both surface pressure and surface potential isotherms became more expanded upon addition of TRP3 (DPPE similar to DPPC << DPPA < DPPG). the stronger interaction with negatively charged phospholipids agrees with data for vesicles and planar lipid bilayers, and with AMPs greater activity against bacterial membranes versus mammalian cell membranes. Considerable expansion of negatively charged monolayers occurred at 10 and 30 mol% TRP3, especially at low surface pressure. Moreover, a difference was observed between PA and PG, demonstrating that the interaction, besides being modulated by electrostatic interactions, displays specificity with regard to headgroup, being more pronounced in the case of PG, present in large quantities in bacterial membranes. in previous studies, it was proposed that the peptide acts by a toroidal pore-like mechanism [1,2]. Considering the evidence from the literature that PG shows a propensity to form a positive curvature as do toroidal pores, the observation of TRP3's preference for the PG headgroup and the dramatic increase in area promoted by this interaction represent further support for the toroidal pore mechanism of action proposed for TRP3. (C) 2012 Elsevier B.V. All rights reserved.
Keywords Tritrpticin
Antimicrobial peptide
Model membranes
Phospholipid monolayers
Toroidal pore
Language English
Sponsor Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
Rede Biomat (Brazil)
Date 2012-12-01
Published in Colloids and Surfaces B-biointerfaces. Amsterdam: Elsevier B.V., v. 100, p. 95-102, 2012.
ISSN 0927-7765 (Sherpa/Romeo, impact factor)
Publisher Elsevier B.V.
Extent 95-102
Origin http://dx.doi.org/10.1016/j.colsurfb.2012.05.002
Access rights Closed access
Type Article
Web of Science ID WOS:000307683900014
URI http://repositorio.unifesp.br/handle/11600/35557

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