2L5R

Conformational and membrane interactins studies of antimicrobial peptide Alyteserin-1C

2L5R の概要

• エントリーDOI: 10.2210/pdb2l5r/pdb
• NMR情報: BMRB: 17281
• 分子名称: Antimicrobial peptide Alyteserin-1C (1 entity in total)
• 機能のキーワード: alpha helix, antimicrobial protein
• 由来する生物種: Alytes obstetricans (midwife toad)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 2270.71

構造登録者

Subasinghage, A.P.,Hewage, C.M.,Conlon, M. (登録日: 2010-11-03, 公開日: 2011-11-23, 最終更新日: 2024-05-01)

主引用文献

Subasinghage, A.P.,O'Flynn, D.,Conlon, J.M.,Hewage, C.M.
Conformational and membrane interaction studies of the antimicrobial peptide alyteserin-1c and its analogue [E4K]alyteserin-1c.
Biochim.Biophys.Acta, 1808:1975-1984, 2011

PubMed Abstract: Alyteserin-1c (GLKEIFKAGLGSLVKGIAAHVAS.NH(2)), first isolated from skin secretions of the midwife toad Alytes obstetricans, shows selective growth-inhibitory activity against Gram-negative bacteria. The structures of alyteserin-1c and its more potent and less haemolytic analogue [E4K]alyteserin-1c were investigated in various solution and membrane mimicking environments by proton NMR spectroscopy and molecular modelling. In aqueous solution, the peptide displays a lack of secondary structure but, in a 2,2,2-trifluoroethanol (TFE-d(3))-H(2)O solvent mixture, the structure is characterised by an extended alpha helix between residues Leu(2) and Val(21). Solution structural studies in the membrane mimicking environments, sodium dodecyl sulphate (SDS), dodecylphosphocholine (DPC), and 1,2-dihexanoyl-sn-glycero-3-phosphatidylcholine (DHPC) micelles, indicate that these peptides display an alpha helical structure between residues Lys(3) and Val(21). Positional studies of the peptides in SDS, DPC and DHPC media show that the N-terminal and central residues lie inside the micelle while C-terminal residues beyond Ala(19) do not interact with the micelles.

PubMed: 21565166
DOI: 10.1016/j.bbamem.2011.04.012

実験手法

SOLUTION NMR