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Novel strategies for targeting the dimerization interface of HIV protease with cross‐linked interfacial peptides
Author(s) -
Bowman Michael J.,
Chmielewski Jean
Publication year - 2002
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.10232
Subject(s) - chemistry , protease , human immunodeficiency virus (hiv) , hiv 1 protease , peptide , potency , monomer , enzyme , biochemistry , combinatorial chemistry , in vitro , virology , medicine , organic chemistry , polymer
As the prevalence of AIDS continues to grow, and current therapeutic agents begin to lose efficacy, the need for alternative treatments to combat HIV has become significantly greater. Targeting the highly conserved dimerization interface of HIV protease (PR) with interfacial peptides has been shown to reduce the activity of the enzyme due to generation of inactive monomers. The potency of these peptide‐based inhibitors has been dramatically increased by cross‐linking the interfacial sequences derived from HIV PR. This review focuses on a variety of strategies to develop potent, low‐molecular‐weight dimerization inhibitors of HIV PR. © 2002 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 66: 126–133, 2002