Journal
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
Volume 1860, Issue 11, Pages 2242-2251Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamem.2018.09.004
Keywords
Lipopeptide; Critical micellar concentration; Self-assembly; FTIR; ITC; Coarse-grained molecular dynamics
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Funding
- National Science Centre in Poland [2016/21/B/ST5/01375]
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In this paper, we examine antimicrobial and cytotoxic activities, self-assembly and interactions with anionic and zwitterionic membranes of short arginine-rich lipopeptides: C-16-RRRR-NH2, C-14-RRRR-NH2, C-52-RRRR-NH2, and C-16-PRRR-NH2. They show a tendency to self-assembly into micelles, but it is not required for antimicrobial activity. The membrane binding of the lipopeptides can be accompanied by other factors such as: peptide aggregation, pore formation or micellization of phospholipid bilayer. The shortening of the acyl chain results in compounds with a lower haemolytic activity and a slightly improved antimicrobial activity against Gram-positive bacteria, what indicates enhanced cell specificity. Results of coarse-grained molecular dynamics simulations indicate different organization of membrane lipids upon binding of arginine-based lipopeptides and the previously studied lysine-based ones.
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