Physiological activities of peptides are correlated with the conformations of membrane‐bound molecules

FEBS Letters

Sakakibara, Shumpei¹  Fujimura, Kuniko²  Miyazawa, Tatsuo²  Higashijima, Tsutomu²  Masui, Yoshihiro¹ 

[1] Peptide Institute, Protein Research Foundation, Minoh-shi, Osaka 562, Japan;Department of Biophysics and Biochemistry, Faculty of Science, University of Tokyo, Bunkyo-ku, Tokyo 113, Japan

关键词: α-Mating factor;    Saccharomyces cerevisiae;    Fluorescence;    Circular dichroism;    Membrane-bound conformation;    Conformation-activity relationship;   

DOI  :  10.1016/0014-5793(83)80452-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

α-Mating factor from Saccharomyces cerevisiae and analog peptides are found, by fluorescence analyses, to interact with phospholipid membrane. The circular dichroism analyses indicate that the physiological activities of α-mating factor and analog peptide are correlated with the conformations of the membrane-bound molecules rather than with the molecular conformations in aqueous solution. This suggests that the conformation change of peptide hormone upon binding with phospholipid membrane is an essential step for the recognition by the receptor.

【 授权许可】

Unknown