Design, synthesis and primary activity assay of bi- or tri-peptide analogues with the scaffold l-arginine as amino-peptidase N/CD13 inhibitors.
A series of bi- or tri-peptide analogues with the scaffold l-arginine were designed, synthesized and evaluated for their inhibitory activities against amino-peptidase N (APN) and metalloproteinase-2 (MMP-2). The primary activity assay showed that all the compounds exhibited higher inhibitory activities against APN than MMP-2. Within this series, compounds C6 and C7 (IC(50)=4.2 and 4.3microM) showed comparable APN inhibitory activities with the positive control bestatin (IC(50)=3.8microM).
Mou
Jiajia
J
Department of Medicinal Chemistry, School of Pharmacy, Shandong University, 44, Wenhuaxi Road, Ji'nan, Shandong 250012, PR China.
Fang
Hao
H
Liu
Yingzi
Y
Shang
Luqing
L
Wang
Qiang
Q
Zhang
Lei
L
Xu
Wenfang
W
D001120:Arginine / Q000737:chemistry*; D018826:CD13 Antigens / Q000037:antagonists & inhibitors*; D018360:Crystallography, X-Ray; D015195:Drug Design; D004791:Enzyme Inhibitors / Q000138:chemical synthesis / Q000737:chemistry / Q000494:pharmacology*; D061965:Matrix Metalloproteinase Inhibitors; D008958:Models, Molecular; D008968:Molecular Conformation; D009842:Oligopeptides / Q000138:chemical synthesis / Q000737:chemistry / Q000494:pharmacology*; D013237:Stereoisomerism; D013329:Structure-Activity Relationship
D004791:Enzyme Inhibitors; D061965:Matrix Metalloproteinase Inhibitors; D009842:Oligopeptides; D001120:Arginine; D018826:CD13 Antigens