Priestley E Scott, De Lucca Indawati, Ghavimi Bahman, Erickson-Viitanen Susan, Decicco Carl P
Bristol-Myers Squibb Pharmaceutical Research Institute, Experimental Station, Wilmington,DE 19880-0500, USA.
Bioorg Med Chem Lett. 2002 Nov 4;12(21):3199-202. doi: 10.1016/s0960-894x(02)00682-0.
A series of peptide boronic acids containing extended, hydrophobic P1 residues was prepared to probe the shallow, hydrophobic S1 region of HCV NS3 protease. The p-trifluoromethylphenethyl P1 substituent was identified as optimal with respect to inhibitor potency for NS3 and selectivity against elastase and chymotrypsin.
制备了一系列含有延伸的疏水P1残基的肽硼酸，以探测丙型肝炎病毒NS3蛋白酶的浅疏水S1区域。就对NS3的抑制效力以及对弹性蛋白酶和胰凝乳蛋白酶的选择性而言，对三氟甲基苯乙基P1取代基被确定为最佳。
