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

Authors :
Salay LC
Ferreira M
Oliveira ON Jr
Nakaie CR
Schreier S
Source :
Colloids and surfaces. B, Biointerfaces [Colloids Surf B Biointerfaces] 2012 Dec 01; Vol. 100, pp. 95-102. Date of Electronic Publication: 2012 May 23.
Publication Year :
2012

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~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. 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.<br /> (Copyright © 2012 Elsevier B.V. All rights reserved.)

Details

Language :
English
ISSN :
1873-4367
Volume :
100
Database :
MEDLINE
Journal :
Colloids and surfaces. B, Biointerfaces
Publication Type :
Academic Journal
Accession number :
22772075
Full Text :
https://doi.org/10.1016/j.colsurfb.2012.05.002