7OVZ

SOLUTION NMR STRUCTURE OF MAXIMIN 1 IN 50% TRIFLUOROETHANOL

7OVZ の概要

• エントリーDOI: 10.2210/pdb7ovz/pdb
• 関連するPDBエントリー: 6HZ2
• NMR情報: BMRB: 34639
• 分子名称: Maximin-1 (1 entity in total)
• 機能のキーワード: maximin 1, antimicrobial peptide, antimicrobial protein
• 由来する生物種: Bombina maxima (Giant fire-bellied toad, Chinese red belly toad)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 2679.16

構造登録者

Timmons, P.B.,Hewage, C.M. (登録日: 2021-06-15, 公開日: 2021-10-13, 最終更新日: 2024-06-19)

主引用文献

Timmons, P.B.,Hewage, C.M.
Biophysical study of the structure and dynamics of the antimicrobial peptide maximin 1.
J.Pept.Sci., 28:e3370-e3370, 2022

PubMed Abstract: Maximin 1 is a cationic, amphipathic antimicrobial peptide found in the skin secretions and brains of the Chinese red belly toad Bombina maxima. The 27 amino acid residue-long peptide is biologically interesting as it possesses a variety of biological activities, including antibacterial, antifungal, antiviral, antitumour and spermicidal activities. Its three-dimensional structural model was obtained in a 50/50% water/2,2,2-trifluoroethanol-d mixture using two-dimensional NMR spectroscopy. Maximin 1 was found to adopt an α-helical structure from residue Ile to Ala . The peptide is amphipathic, showing a clear separation between polar and non-polar residues. The interactions with sodium dodecyl sulfate micelles, a widely-used bacterial membrane-mimicking environment, were modelled using molecular dynamics simulations. The peptide maintains an α-helical conformation, occasionally displaying a flexibility around the Gly and Gly residues, which is likely responsible for the peptide's low haemolytic activity. It is found to preferentially adopt a position parallel to the micellar surface, establishing a number of hydrophobic and electrostatic interactions with the micelle.

PubMed: 34569121
DOI: 10.1002/psc.3370

実験手法

SOLUTION NMR