Synthesis, conformation, and antibody recognition of peptides built of the sequence of the flap of human renin

✍ Scribed by Chuan Fa Liu; Jean-Alain Fehrentz; Annie Heitz; Dung Le Nguyen; Bertrand Castro; Frédéric Heitz; Claude Carelli; François-Xavier Galen; Plerre Corvol

• Book ID: 104203719
• Publisher: Elsevier Science
• Year: 1988
• Tongue: French
• Weight: 566 KB
• Volume: 44
• Category: Article
• ISSN: 0040-4020
• DOI: 10.1016/s0040-4020(01)86108-1

✦ Synopsis

Flve peptides related to human renin flap region have been synthesized. Two of them are ring cbsed through properly designed dlsulfkie bridges. Structure analysis Involving IR, CD and NMR techniques and recognition by antibodies raised against human renin support our assumption that in the protein, the flap region adopts a 6 and y turn leading to the carbonyl group of residue 83 (Tyr) interacting with the NH's of residues 85 (Thr) and 86 (Gly).

Understanding of protein function at the molecular level requires knowledge of the detalled three dimensional structure of the protein. Up to now, in spite of numerous structural studies including mainly X-ray diffraction and two dimensional NMR spectroscopy which require large amounts of material (i.e. me), the precise conformation 01 many proteins is still unknown. Attempts to overcome these experimental difficulties have been developed and are based on structure prediction and conformational investigations on synthetic peptides mimicking fragments of proteins. For