5M9U

Spatial structure of antimicrobial peptide arenicin-1 mutant V8R

5M9U の概要

• エントリーDOI: 10.2210/pdb5m9u/pdb
• NMR情報: BMRB: 34059
• 分子名称: Arenicin-1 (1 entity in total)
• 機能のキーワード: structure from cyana 3.97, antimicrobial protein
• 由来する生物種: Arenicola marina (Lugworm)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 2824.41

構造登録者

Myshkin, M.Y.,Shenkarev, Z.O.,Panteleev, P.V.,Ovchinnikova, T.V. (登録日: 2016-11-02, 公開日: 2017-07-26, 最終更新日: 2024-11-06)

主引用文献

Panteleev, P.V.,Myshkin, M.Y.,Shenkarev, Z.O.,Ovchinnikova, T.V.
Dimerization of the antimicrobial peptide arenicin plays a key role in the cytotoxicity but not in the antibacterial activity.
Biochem. Biophys. Res. Commun., 482:1320-1326, 2017

PubMed Abstract: The β-hairpin antimicrobial peptides arenicins from marine polychaeta Arenicola marina exhibit a broad spectrum of antimicrobial activity and high cytotoxicity. In this study the biological activities of arenicin-1 and its therapeutically valuable analog Ar-1[V8R] were investigated. The peptide Ar-1[V8R] displays significantly reduced cytotoxicity against mammalian cells relative to the wild-type arenicin-1. At the same time, both peptides exhibit similar antibacterial activities and kinetics of bacterial membrane permeabilization. Comparative NMR analysis of the peptides spatial structures in water and membrane-mimicking environment showed that Ar-1[V8R] in contrast to arenicin has significantly lower dimerization propensity. Thus, dimerization of the antimicrobial peptide arenicin plays a key role in the cytotoxicity but not in the antibacterial activity.

PubMed: 27940358
DOI: 10.1016/j.bbrc.2016.12.035

実験手法

SOLUTION NMR