1XV7

Solution structure of antimicrobial and endotoxin-neutralizing peptide Lf11 in DPC micelles

1XV7 の概要

• エントリーDOI: 10.2210/pdb1xv7/pdb
• 関連するPDBエントリー: 1XV4
• 分子名称: lactoferrin-based synthetic peptide FQWQRNIRKVR (1 entity in total)
• 機能のキーワード: loop, hydrophobic core, metal transport
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 1532.82

構造登録者

Japelj, B.,Pristovsek, P.,Majerle, A.,Jerala, R. (登録日: 2004-10-27, 公開日: 2005-03-22, 最終更新日: 2024-10-23)

主引用文献

Japelj, B.,Pristovsek, P.,Majerle, A.,Jerala, R.
Structural origin of endotoxin neutralization and antimicrobial activity of a lactoferrin-based peptide
J.Biol.Chem., 280:16955-16961, 2005

PubMed Abstract: Treatment of Gram-negative bacterial infections with antimicrobial agents can cause release of the endotoxin lipopolysaccharide (LPS), the potent initiator of sepsis, which is the major cause of mortality in intensive care units worldwide. Structural information on peptides bound to LPS can lead to the development of more effective endotoxin neutralizers. Short linear antimicrobial and endotoxin-neutralizing peptide LF11, based on the human lactoferrin, binds to LPS, inducing a peptide fold with a "T-shaped" arrangement of a hydrophobic core and two clusters of basic residues that match the distance between the two phosphate groups of LPS. Side chain arrangement of LF11 bound to LPS extends the previously proposed LPS binding pattern, emphasizing the importance of both electrostatic and hydrophobic interactions in a defined geometric arrangement. In anionic micelles, the LF11 forms amphipathic conformation with a smaller hydrophobic core than in LPS, whereas in zwitterionic micelles, the structure is even less defined. Protection of tryptophan fluorescence quenching in the order SDS>LPS>DPC and hydrogen exchange protection indicates the decreasing extent of insertion of the N terminus and potential role of peptide plasticity in differentiation between bacterial and eukaryotic membranes.

PubMed: 15687491
DOI: 10.1074/jbc.M500266200

実験手法

SOLUTION NMR