Synthesis and circular dichroism study of the human salivary proline-rich protein IB7

J Pept Sci. 2003 Feb;9(2):125-31. doi: 10.1002/psc.438.

Abstract

The solid phase synthesis of a 59 amino acid human salivary protein IB7 has been accomplished using Fmoc strategy. Because the protein contains 25 proline, 13 glycine and 9 glutamine residues the coupling time, piperidine delivery and acetic anhydride reaction time were increased. Yield after HPLC purification was 35%. Circular dichroism studies revealed that about one third of IB7 residues adopted a type II helix secondary structure, as found in collagen helices. The rest of the sequence adopts a random coil secondary structure.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Circular Dichroism*
  • Humans
  • Molecular Sequence Data
  • Peptides / chemical synthesis*
  • Peptides / chemistry*
  • Peptides / isolation & purification
  • Proline-Rich Protein Domains
  • Protein Structure, Secondary
  • Salivary Proteins and Peptides / chemical synthesis*
  • Salivary Proteins and Peptides / chemistry*
  • Salivary Proteins and Peptides / isolation & purification

Substances

  • Peptides
  • Salivary Proteins and Peptides