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Bioactive peptides: Conformational studies of [TYR4] cyclolinopeptide A

✍ Scribed by Michele Saviano; Filomena Rossi; Marta Filizola; Carla Isernia; Benedetto Di Blasio; Ettore Benedetti; Carlo Pedone; Ignacy Z. Siemion; Artur Pedyczak

Book ID: 102765304
Publisher: Wiley (John Wiley & Sons)
Year: 1995
Tongue: English
Weight: 591 KB
Volume: 36
Category: Article
ISSN: 0006-3525
DOI: 10.1002/bip.360360408

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Cyclolinopeptide A, a cyclic nonapeptide, was isolated in 1956 from linseed oil.' In 1966 Prox and Weygand' determined the amino acid composition and they elucidated the sequence of the peptide, demonstrating the following chemical structure: \*Dedicated to the memory of Professor F. Weygand.

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Ion binding of cyclolinopeptide A: An nm

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## SYNOPSIS CD and nmr techniques have been used to study, in acetonitrile solution, the ion-complexing capability of cyclolinopeptide A (CLA) , a cyclic nonapeptide of sequence cyclo-( Pro-Pro-Phe-Phe-Leu-Ile-Ile-Leu-Val) endowed with remarkable cytoprotective ability in vitro, and the conformati

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The side chain of T w and Phe was,fixed into the gauche (-) or gauche (+) conjormation by using the Tic or Htc structura, and into the trans conformation by using an aminobenzazepine-t)~e (Aha) structure. When incorporated into dermorphin or deltorphin II, the Tic and Htc analogues all showed a larg