Spatial organization and conformational peculiarities of the callatostatin family of neuropeptides | Zendy

Alieva I. N. | Zendy; Velieva L. I. | Zendy; Aliev D. I. | Zendy; Godjaev N. M. | Zendy

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Spatial organization and conformational peculiarities of the callatostatin family of neuropeptides

Author(s) -

Alieva I. N.,

Velieva L. I.,

Aliev D. I.,

Godjaev N. M.

Publication year - 2002

Publication title -

journal of peptide science

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.475

H-Index - 66

eISSN - 1099-1387

pISSN - 1075-2617

DOI - 10.1002/psc.389

Subject(s) - pentapeptide repeat , conformational isomerism , chemistry , amino acid residue , stereochemistry , neuropeptide , conformational change , peptide , biophysics , biochemistry , peptide sequence , biology , molecule , organic chemistry , receptor , gene

The structures and conformational peculiarities of five members of the callatostatin family of neuropeptides, i.e. Leu‐ and Met‐callatostatins, ranging in size from 8 to 16 amino acid residues have been investigated by a theoretical conformational analysis method. A comparative analysis of the conformational flexibilities of Met‐callatostatin with those of the hydroxylated analogues, [Hyp 2 ]‐ and [Hyp 3 ]‐ Met‐callatostatin has been carried out. Helically packed C ‐terminal pentapeptide in the structure of all investigated Leu‐callatostatins are shown to be possible. The reason for the great number low‐energy conformers for the callatostatin N ‐terminus is discussed. Copyright © 2002 European Peptide Society and John Wiley & Sons, Ltd.

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