2N0O

NMR Solution Structure and Model Membrane Interaction Studies of the Peptide Hylin a1 from the Arboreal South American Frog Hypsiboas albopunctatus

2N0O の概要

• エントリーDOI: 10.2210/pdb2n0o/pdb
• NMR情報: BMRB: 25529
• 分子名称: Hylin-a1 (1 entity in total)
• 機能のキーワード: antimicrobial protein
• 由来する生物種: Hypsiboas albopunctatus (Spotted tree frog)
• 細胞内の位置: Secreted : P85982
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 1865.37

構造登録者

Alves, E.S.F.,Oliveira, A.L. (登録日: 2015-03-11, 公開日: 2015-06-24, 最終更新日: 2024-10-09)

主引用文献

Alves, E.S.,Junior, E.C.,Cilli, E.M.,Castro, M.S.,Fontes, W.,de Magalhaes, M.T.,Liao, L.M.,de Oliveira, A.L.
Micelle Bound Structure and Model Membrane Interaction Studies of the Peptide Hylin a1 from the Arboreal South American Frog Hypsiboas albopunctatus.
Protein Pept.Lett., 22:719-726, 2015

PubMed Abstract: Antimicrobial peptides (AMPs) appear as a promising therapeutic candidate against multiresistant pathogens, because they are able to kill microorganisms and have low toxicity of resistance cells. Hylin a1 (Hy-a1, IFGAILPLALGALKNLIK-NH2) is a peptide extracted from the skin secretion of the frog Hypsiboas albopunctatus, which displays antimicrobial and hemolytic activities. We report here structural studies of Hy-a1 using different techniques such as fluorescence, CD and NMR. Our data showed that Hy-a1 acquires a well defined amphipathic α-helix when interacting with a membrane-like environment. Furthermore, Hy-a1 presented different affinity when compared to membranes of zwitterionic or anionic lipid composition. Finally, we proposed a molecular interaction model of this peptide with micelles.

PubMed: 26059694

実験手法

SOLUTION NMR