Structure-activity relationships for mini atrial natriuretic peptide by proline-scanning mutagenesis and shortening
Kenji Sugase1, Yoshiaki Oyama, Katsuhiko Kitano
1Suntory Institute for Bioorganic Research, Shimamoto, 618-8503, Mishima, Japan.
Bioorganic & Medicinal Chemistry Letters
|April 20, 2002
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.
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