Headgroup specificity for the interaction of the antimicrobial peptide tritrpticin with phospholipid Langmuir
Luiz C Salay1, Marystela Ferreira, Osvaldo N Oliveira
1Department of Biochemistry, Institute of Chemistry, University of São Paulo, São Paulo, SP, Brazil.
Colloids and Surfaces. B, Biointerfaces
|July 10, 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<

