Dermcidin, an anionic antimicrobial peptide: influence of lipid charge, pH and Zn2+on its interaction with a biomimetic membrane
Author:
Publisher
Royal Society of Chemistry (RSC)
Subject
Condensed Matter Physics,General Chemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2014/SM/C3SM52400K
Reference46 articles.
1. Dermcidin: a novel human antibiotic peptide secreted by sweat glands
2. Functional and structural characterization of recombinant dermcidin-1L, a human antimicrobial peptide
3. Structure-Activity Analysis of the Dermcidin-derived Peptide DCD-1L, an Anionic Antimicrobial Peptide Present in Human Sweat
4. Naturally Processed Dermcidin-Derived Peptides Do Not Permeabilize Bacterial Membranes and Kill Microorganisms Irrespective of Their Charge
5. Effects of the phosphatidylglycerol head group on the binding of short dermcidin-derived peptides to the phospholipid membrane surface
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