6TWG

Solution structure of antimicrobial peptide, crabrolin Plus in the presence of Lipopolysaccharide

6TWG の概要

• エントリーDOI: 10.2210/pdb6twg/pdb
• NMR情報: BMRB: 34476
• 分子名称: Crabrolin Plus, mutant of Crabrolin peptide (1 entity in total)
• 機能のキーワード: antimicrobial peptide, lipopolysaccharide, antimicrobial protein
• 由来する生物種: Vespa crabro (European hornet)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 1571.05

構造登録者

Cantini, F.,Bouchemal, N.,Savarin, P.,Sette, M. (登録日: 2020-01-13, 公開日: 2020-07-22, 最終更新日: 2024-06-19)

主引用文献

Cantini, F.,Luzi, C.,Bouchemal, N.,Savarin, P.,Bozzi, A.,Sette, M.
Effect of positive charges in the structural interaction of crabrolin isoforms with lipopolysaccharide.
J.Pept.Sci., 26:e3271-e3271, 2020

PubMed Abstract: Antimicrobial peptides (AMPs) appear as chemical compounds of increasing interest for their role in killing bacteria and, more recently, for their ability to bind endotoxin (lipopolysaccharide, LPS) that is released during bacterial infection and that may lead to septic shock. This dual role in the mechanism of action can further be enhanced in a synergistic way when two or more AMPs are combined together. Not all AMPs are able to bind LPS, suggesting that several modes of binding to the bacterial surface may exist. Here we analyze a natural AMP, crabrolin, and two mutated forms, one with increased positive charge (Crabrolin Plus) and the other with null charge (Crabrolin Minus), and compare their binding abilities to LPS. While Crabrolin WT as well Crabrolin Minus do not show binding to LPS, the mutated Crabrolin Plus exhibits binding and forms a well defined structure in the presence of LPS. The results strengthen the importance of positive charges for the binding to LPS and suggest the mutated form with increased positive charge as a promising candidate for antimicrobial and antiseptic activity.

PubMed: 32585759
DOI: 10.1002/psc.3271

実験手法

SOLUTION NMR