Spatial organization and conformational peculiarities of the callatostatin family of neuropeptides

✍ Scribed by I. N. Alieva; L. I. Velieva; Dr D. I. Aliev; N. M. Godjaev

• Publisher: John Wiley and Sons
• Year: 2002
• Tongue: English
• Weight: 130 KB
• Volume: 8
• Category: Article
• ISSN: 1075-2617
• DOI: 10.1002/psc.389

✦ Synopsis

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, [Hyp2]- and [Hyp3]-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.