1QWP

NMR analysis of 25-35 fragment of beta amyloid peptide

1QWP の概要

• エントリーDOI: 10.2210/pdb1qwp/pdb
• 関連するPDBエントリー: 1IYT
• 分子名称: 11-mer peptide from Amyloid beta A4 protein (1 entity in total)
• 機能のキーワード: amyloid beta peptide- kink structure, protein binding
• 細胞内の位置: Membrane; Single-pass type I membrane protein: P05067
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 1061.28

構造登録者

D'Ursi, A.M.,Armenante, M.R.,Guerrini, R.,Salvadori, S.,Sorrentino, G.,Picone, D. (登録日: 2003-09-03, 公開日: 2004-09-14, 最終更新日: 2024-05-29)

主引用文献

D'Ursi, A.M.,Armenante, M.R.,Guerrini, R.,Salvadori, S.,Sorrentino, G.,Picone, D.
Solution structure of amyloid beta-peptide (25-35) in different media
J.Med.Chem., 47:4231-4238, 2004

PubMed Abstract: The design of molecules able to interact with the amyloid peptides either as inhibitors of fibril formation or as inhibitors of amyloid membrane pore formation represents one of the most relevant approaches in the development of anti-Alzheimer therapies. Abeta-(25-35), sequence GSNKGAIIGLM, is a highly toxic synthetic derivative of amyloid beta-peptides (Abeta-peptides), which forms fibrillary aggregates. Here, we report the NMR and CD investigation of Abeta-(25-35) in a membrane-mimicking environment and in isotropic mixtures of water and fluoro-alcohols to scan its conformational properties as a function of the medium. The analysis of the 3D structures in the mentioned conditions indicates a propensity of the peptide to behave as a typical transmembrane helix in the lipidic environment. In media characterized by different polarity, it loses the structural regularity at specific points of the sequence as a function of the environment. Furthermore, a comparison with the solution structure of full-length amyloid peptides suggests a role for the 25-27 kink region, which appears to be a general feature of all peptides under the solution conditions explored.

PubMed: 15293994
DOI: 10.1021/jm040773o

実験手法

SOLUTION NMR