5NES

Discovery, crystal structures and atomic force microscopy study of thioether ligated D,L-cyclic antimicrobial peptides against multidrug resistant Pseudomonas aeruginosa

5NES の概要

• エントリーDOI: 10.2210/pdb5nes/pdb
• 分子名称: Fucose-binding lectin II (PA-IIL), CYD-TRP-TRD-LYS-LYD-LYS-LYD-LYS-TRD-TRP-CYD, CALCIUM ION, ... (6 entities in total)
• 機能のキーワード: cyclic peptides, antimicrobials, pseudomonas aeruginosa, sugar binding protein
• 由来する生物種: Pseudomonas aeruginosa; 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 49803.41

構造登録者

Reymond, J.-L.,Darbre, T.,Stocker, A.,Hong, W.,van Delden, C.,Koehler, T.,Luscher, A.,Visini, R.,Fu, Y.,Di Bonaventura, I.,He, R. (登録日: 2017-03-11, 公開日: 2017-09-13, 最終更新日: 2024-01-17)

主引用文献

He, R.,Di Bonaventura, I.,Visini, R.,Gan, B.H.,Fu, Y.,Probst, D.,Luscher, A.,Kohler, T.,van Delden, C.,Stocker, A.,Hong, W.,Darbre, T.,Reymond, J.L.
Design, crystal structure and atomic force microscopy study of thioether ligated d,l-cyclic antimicrobial peptides against multidrug resistant Pseudomonas aeruginosa.
Chem Sci, 8:7464-7475, 2017

PubMed Abstract: Here we report a new family of cyclic antimicrobial peptides (CAMPs) targeting MDR strains of . These CAMPs are cyclized a xylene double thioether bridge connecting two cysteines placed at the ends of a linear amphiphilic alternating d,l-sequence composed of lysines and tryptophans. Investigations by transmission electron microscopy (TEM), dynamic light scattering and atomic force microscopy (AFM) suggest that these peptide macrocycles interact with the membrane to form lipid-peptide aggregates. Amphiphilic conformations compatible with membrane disruption are observed in high resolution X-ray crystal structures of fucosylated derivatives in complex with lectin LecB. The potential for optimization is highlighted by -methylation of backbone amides leading to derivatives with similar antimicrobial activity but lower hemolysis.

PubMed: 29163899
DOI: 10.1039/c7sc01599b

実験手法

X-RAY DIFFRACTION (1.606 Å)