Peptides related to the active fragment of "proline rich polypeptide", an immunoregulatory protein of the ovine colostrum. Spectroscopic and computer modeling studies

I Z Siemion; G Folkers; Z Szewczuk; A Jankowski; A Kubik; W Voelter

Peptides related to the active fragment of "proline rich polypeptide", an immunoregulatory protein of the ovine colostrum. Spectroscopic and computer modeling studies

Int J Pept Protein Res. 1990 Dec;36(6):506-14.

Authors

I Z Siemion¹, G Folkers, Z Szewczuk, A Jankowski, A Kubik, W Voelter

Affiliation

¹ Institute of Chemistry, Wroclaw University, Poland.

PMID: 2090642

Abstract

The preferred solution conformation of the PRP-hexapeptide (Tyr-Val-Pro-Leu-Phe-Pro) and of some of its structural analogues was investigated by NMR-spectroscopy, spectrofluorimetry and computer simulation technic. It was found that the preferred conformation is characterized by cis'-conformation of Pro3 and the gamma-turn on the Leu4-residue: for Val2 and Phe5 a beta-structure seems to be privileged. In such a conformation Val2 and Leu4 residues occupy exactly the same positions in space as residues i and i + 3 in an alpha-helix. It suggests that the PRP-hexapeptide can interact with receptor protein inducing or stabilizing its helical conformation by "knobs into holes" packing.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Animals
Colostrum / chemistry*
Female
Magnetic Resonance Spectroscopy / methods
Molecular Sequence Data
Peptide Fragments / chemistry*
Peptides / chemistry*
Peptides / physiology
Pregnancy
Proline-Rich Protein Domains
Protein Conformation
Sheep

Substances

Peptide Fragments
Peptides