title: Probing the role of interfacial residues in a dimerization inhibitor of HIV-1 protease.
abstract: 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.
authors.affiliation: Department of Chemistry, Purdue University, West Lafayette, IN 47907, USA.
authors.forename: M D
authors.initials: MD
authors.lastname: Shultz
authors.forename: J
authors.initials: J
authors.lastname: Chmielewski
mesh_terms: D000409:Alanine / Q000737:chemistry; D019943:Amino Acid Substitution; D019281:Dimerization; D017320:HIV Protease Inhibitors / Q000737:chemistry*; D015497:HIV-1 / Q000201:enzymology
chemical_list: D017320:HIV Protease Inhibitors; D000409:Alanine