7BX2

The solution NMR structure of VV14 peptide in the presence of Deuterated SDS micelle.

7BX2 の概要

• エントリーDOI: 10.2210/pdb7bx2/pdb
• NMR情報: BMRB: 36347
• 分子名称: VAL-LYS-TRP-VAL-LYS-LYS-VAL-VAL-LYS-TRP-VAL-LYS-LYS-VAL (1 entity in total)
• 機能のキーワード: structure from cyana 2.1, antimicrobial peptide, sds micelle, alpha helix., antimicrobial protein
• 由来する生物種: synthetic construct
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 1760.30

構造登録者

Bhunia, A.,Mohid, S.A.,Chowdhury, N. (登録日: 2020-04-16, 公開日: 2021-04-21, 最終更新日: 2024-05-15)

主引用文献

Pandit, G.,Chowdhury, N.,Abdul Mohid, S.,Bidkar, A.P.,Bhunia, A.,Chatterjee, S.
Effect of Secondary Structure and Side Chain Length of Hydrophobic Amino Acid Residues on the Antimicrobial Activity and Toxicity of 14-Residue-Long de novo AMPs.
Chemmedchem, 16:355-367, 2021

PubMed Abstract: Herein we report the efficacy and toxicity of three de novo designed cationic antimicrobial peptides (AMPs) LL-14, VV-14 and ββ-14, where side chains of the hydrophobic amino acids were reduced gradually. The AMPs showed broad-spectrum antimicrobial activity against three pathogens from the ESKAPE group and two fungal strains. This study showed that side chains which are either too long or too short increase toxicity and lower antimicrobial activity, respectively. VV-14 was found to be non-cytotoxic and highly potent under physiological salt concentrations against several pathogens, especially Salmonella typhi TY2. These AMPs acted via membrane deformation, depolarization, and lysis. The activity of the AMPs is related to their ability to take on amphipathic helical conformations in the presence of microbial membrane mimics. Among AMPs with the same charge, hydrophobic interactions between the side chains of the residues with cell membrane lipids determine their antimicrobial potency and cytotoxicity. Strikingly, an optimum hydrophobic interaction is the crux of generating highly potent non-cytotoxic AMPs.

PubMed: 33026188
DOI: 10.1002/cmdc.202000550

実験手法

SOLUTION NMR