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

Autor: Shultz MD; Department of Chemistry, Purdue University, West Lafayette, IN 47907, USA., Chmielewski J
Jazyk: angličtina
Zdroj: Bioorganic & medicinal chemistry letters [Bioorg Med Chem Lett] 1999 Aug 16; Vol. 9 (16), pp. 2431-6.
DOI: 10.1016/s0960-894x(99)00400-x
Abstrakt: 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.
Databáze: MEDLINE