Title of article :
Structure–activity relationships for mini atrial natriuretic peptide by proline-Scanning mutagenesis and shortening of peptide backbone
Author/Authors :
Kenji Sugase، نويسنده , , Yoshiaki Oyama، نويسنده , , Katsuhiko Kitano، نويسنده , , Hideo Akutsu، نويسنده , , Masaji Ishiguro، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 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.
Journal title :
Bioorganic & Medicinal Chemistry Letters
Journal title :
Bioorganic & Medicinal Chemistry Letters