Short arginine-rich lipopeptides: from self-assembly to antimicrobial activity
Emilia Sikorska , Oktawian Stachurski , Damian Neubauer , Izabela Małuch , Dariusz Wyrzykowski , Marta Bauer , Krzysztof Brzozowski , Wojciech Kamysz
AbstractIn this paper, we examine antimicrobial and cytotoxic activities, self-assembly and interactions with anionic and zwitterionic membranes of short arginine-rich lipopeptides: C16-RRRR-NH2, C14-RRRR-NH2, C12-RRRR-NH2, and C16-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.
|Journal series||Biochimica et Biophysica Acta-Biomembranes, ISSN 0005-2736, (A 35 pkt)|
|Publication size in sheets||0.5|
|Keywords in English||lipopeptide, critical micellar concentration, self-assembly, FTIR, ITC, coarse-grained molecular dynamics|
|Score|| = 35.0, ArticleFromJournal|
= 35.0, ArticleFromJournal
|Publication indicators||: 2017 = 3.438 (2) - 2017=3.64 (5)|
* presented citation count is obtained through Internet information analysis and it is close to the number calculated by the Publish or Perish system.