Probing the role of interfacial residues in a dimerization inhibitor of HIV-1 protease

被引：17

作者：

Shultz, MD ^{[1
]}

Chmielewski, J ^{[1
]}

机构：

[1] Purdue Univ, Dept Chem, W Lafayette, IN 47907 USA

来源：

BIOORGANIC & MEDICINAL CHEMISTRY LETTERS | 1999年 / 9卷 / 16期

关键词：

D O I：

10.1016/S0960-894X(99)00400-X

中图分类号：

R914 [药物化学];

学科分类号：

100701 ;

摘要：

The importance of each side chain of a cross-linked interfacial peptide inhibitor of HIV-1 protease was evaluated using an alanine scanning approach. Whereas the parent inhibitor has an IC50 value of 350 nM, values for the mutations reported here range from 280 - 9200 nM. The relative importance or each residue was thus assigned and correlated to the solvent accessible surface area (SASA) exposed upon mutation. (C) 1999 Elsevier Science Ltd. All rights reserved.

引用

页码：2431 / 2436

页数：6