Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/6409
Title: Dermcidin, an anionic antimicrobial peptide: influence of lipid charge, pH and Zn2+ on its interaction with a biomimetic membrane
Authors: Becucci, Lucia
Valensin, Daniela 
Innocenti, Massimo
Guidelli, Rolando
Keywords: Anti-Infective Agents; Hydrogen-Ion Concentration; Lipid Bilayers; Peptides; Phosphatidylcholines; Phosphatidylserines; Static Electricity; Zinc
Issue Date: 2014
Project: None 
Journal: SOFT MATTER
Abstract: 
The mechanism of membrane permeabilization by dermcidin (DCD-1L), an antimicrobial peptide present in human sweat, was investigated at a mercury-supported monolayer of dioleoylphosphatidylcholine (DOPC) or dioleoylphosphatidylserine (DOPS) and at a mercury-supported tethered bilayer lipid membrane (tBLM) consisting of a thiolipid (DPTL) with a DOPC or DOPS monolayer self-assembled on top of it. In an unbuffered solution of pH 5.4, DCD-1L is almost neutral and permeabilizes a DPTL/DOPS tBLM at transmembrane potentials, ϕtrans, which are physiological. In a pH 7 buffer solution DCD-1L bears two negative charges and has no effect on a DPTL/DOPC tBLM, whereas it permeabilizes a DPTL/DOPS tBLM only outside the physiological ϕtrans range; however, the presence of zinc ion induces DCD-1L to permeabilize the DPTL/DOPS tBLM at physiological ϕtrans values. The effect of zinc ions suggests a DCD-1L conformation with its positive N-terminus embedded in the lipid bilayer and the negative C terminus floating on the membrane surface. This conformation can be stabilized by a zinc ion bridge between the His(38) residue of the C terminus and the carboxyl group of DOPS. Chronocoulometric potential jumps from ϕtrans ≅ +160 mV to sufficiently negative values yield charge transients exhibiting a sigmoidal shape preceded by a relatively long "foot". This behavior is indicative of ion-channel formation characterized by disruption of DCD-1L clusters adsorbed on top of the lipid bilayer, incorporation of the resulting monomers and their aggregation into hydrophilic pores by a mechanism of nucleation and growth.
Description: 
63595
URI: http://hdl.handle.net/20.500.12779/6409
ISSN: 1744-683X
DOI: 10.1039/c3sm52400k
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