Spatial organization and conformational peculiarities of the callatostatin family of neuropeptides

Abstract

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.

Conformational Features of the Dippu-AST 8 Neuropeptide from the Cockroach Diploptera punctata

“…Along with the total energy of a conformation, energy contributions of backbone interactions, interactions within a residue, interactions between side chains and backbone-side chain interactions were considered. The basic principles of the calculation model are presently confirmed by calculations of peptide molecules and of a number of protein fragments and are supported by experimental evidence [18][19][20][21].…”