Structure-activity relationships for mini atrial natriuretic peptide by proline-scanning mutagenesis and shortening of peptide backbone

Bioorg Med Chem Lett. 2002 May 6;12(9):1245-7. doi: 10.1016/s0960-894x(02)00148-8.

Abstract

MiniANP is a synthetic pentadecapeptide analogue of atrial natriuretic polypeptide (ANP). We have used the proline-scanning mutagenesis and the analogue peptides with shorter backbones to characterize the turn-like conformation at residue 6-9 and an extended structure of Gly5-Gly6 as the receptor-bound structure of miniANP. A docking study of miniANP at the binding site of the type A natriuretic peptide receptor (NPR-A) supported the deduced conformation in the receptor-bound structure.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Atrial Natriuretic Factor / chemistry*
  • Atrial Natriuretic Factor / genetics
  • Atrial Natriuretic Factor / pharmacology*
  • CHO Cells
  • Cricetinae
  • Molecular Sequence Data
  • Mutagenesis
  • Proline / chemistry*

Substances

  • Atrial Natriuretic Factor
  • Proline