α‐Bungarotoxin binding to two acetylcholine receptor α‐peptides and their methylmercury‐modified analogs: Intrinsic phosphorescence and optically detected magnetic resonance studies

FEBS Letters

Hawrot, Edward¹  Schlyer, Bruce D.²  Maki, August H.² 

[1] Section of Molecular and Biochemical Pharmacology, Division of Biology and Medicine, Brown University, Providence, RI 02912, USA;Departments of Chemistry, University of California, Davis, CA 95616, USA

关键词: ODMR spectroscopy;    Phosphorescence;    Neurotoxin-acetylcholine receptor interaction;    Heavy-atom modification;   

DOI  :  10.1016/0014-5793(92)80333-C

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Phosphorescence and optically detected magnetic resonance (ODMR) have been used to characterize two synthetic peptides, α181-198 and α185-196, of the major binding determinant of the α-acetylcholine receptor (AChR) of Torpedo californica and its interaction with α-bungarotoxin (BgTX) using Trp as an intrinsic probe. BgTX conformational changes are suggested upon complexation with the peptides. Methylmercury- modified peptides show conformational heterogeneity which brings some of the modified Cys residues into proximity of peptide Trp(s). These modified peptides, when bound to BgTX, undergo structural changes which remove the tagged Cys from its close contact with the Trp residue(s) of the peptide.

【 授权许可】

Unknown