Phosphorescence and ODMR study of the binding interactions of acetylcholine receptor α‐subunit peptides with α‐cobratoxin

FEBS Letters

Pearce, Suman Frieda A.²  Hawrot, Edward¹  Tringali, Arthur E.³  Brenner, Henry C.³ 

[1] Division of Biology and Medicine, Brown University, Providence, RI 02912, USA;Division of Hematology-Oncology, Department of Medicine, Cornell Medical School, 1300 York Avenue, New York, NY 10021, USA;Department of Chemistry, New York University, New York, NY 1003, USA

关键词: Phosphorescence;    ODMR spectroscopy;    Neuroloxin-acetylcholine receptor interaction;   

DOI  :  10.1016/0014-5793(92)81279-U

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Optical detection of magnetic resonance (ODMR) and phosphorescence spectroscopy have been applied to synthetic peptides derived from the α-subunit of the nicotinic acetylcholine receptor of Torpeda californica and their complexes with α-cobratoxin (CBTX). TheCBTX Trp phosphorescence is strongly quenched by the proximal disulfide linkage, while the emission wavelengths and ODMR frequencies of the 18-mer αl81–198 indicate a more hydrophobic Trp environment than in the 12-mer α185–196. Binding to CBTX produces a subtle increase in the hydrophobicity of the Trp environment for the peptides, in qualitative agreement with a recently proposed binding model, in which a receptor Trp residue interacts strongly with a hydrophobic cleft of the toxin.

【 授权许可】

Unknown