6FS4

NMR structure of Casocidin-II antimicrobial peptide in 60% TFE

6FS4 の概要

• エントリーDOI: 10.2210/pdb6fs4/pdb
• 関連するPDBエントリー: 6FS5
• NMR情報: BMRB: 34237
• 分子名称: Alpha-S2-casein (1 entity in total)
• 機能のキーワード: antimicrobial peptide, tfe, antimicrobial protein
• 由来する生物種: Bos taurus (Bovine)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 3864.53

構造登録者

Mercurio, F.A.,Leone, M. (登録日: 2018-02-19, 公開日: 2018-10-03, 最終更新日: 2024-06-19)

主引用文献

Mercurio, F.A.,Scaloni, A.,Caira, S.,Leone, M.
The antimicrobial peptides casocidins I and II: Solution structural studies in water and different membrane-mimetic environments.
Peptides, 114:50-58, 2019

PubMed Abstract: Antimicrobial peptides (AMPs) represent crucial components of the natural immune defense machinery of different organisms. Generally, they are short and positively charged, and bind to and destabilize bacterial cytoplasmic membranes, ultimately leading to cell death. Natural proteolytic cleavage of α-casein in bovine milk generates the antimicrobial peptides casocidin I and II. In the current study, we report for the first time on a detailed structure characterization of casocidins in solution by means of Nuclear Magnetic Resonance spectroscopy (NMR). Structural studies were conducted in HO and different membrane mimetic environments, including 2,2,2-trifluoroethanol (TFE) and lipid anionic and zwitterionic vesicles. For both peptides, results indicate a mainly disordered conformation in HO, with a few residues in a partial helical structure. No wide increase of order occurs upon interaction with lipid vesicles. Conversely, peptide conformation becomes highly ordered in presence of TFE, with both casocidins presenting a large helical content. Our data point out a preference of casocidins to interact with model anionic membranes. These results are compatible with possible mechanisms of action underlying the antimicrobial activity of casocidins that ultimately may affect membrane bilayer stability.

PubMed: 30243923
DOI: 10.1016/j.peptides.2018.09.004

実験手法

SOLUTION NMR