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Protease‐resistant peptide design—empowering nature's fragile warriors against HIV
Author(s) -
Weinstock Matthew T.,
Francis J. Nicholas,
Redman Joseph S.,
Kay Michael S.
Publication year - 2012
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.22073
Subject(s) - chemistry , protease , human immunodeficiency virus (hiv) , peptide , virology , biochemistry , enzyme , biology
Peptides have great potential as therapeutic agents, but their use is often limited by susceptibility to proteolysis and their resulting in vivo fragility. In this review, we focus on peptidomimetic approaches to produce protease‐resistant peptides with the potential for greatly improved clinical utility. We focus on the use of mirror‐image (D‐peptide) and ß‐peptides as two leading approaches with distinct design principles and challenges. Application to the important and difficult problem of inhibiting HIV entry illustrates the current state‐of‐the‐art in peptidomimetic technologies. We also summarize future directions for this field and highlight remaining obstacles to widespread use of protease‐resistant peptides. © 2012 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 98: 431–442, 2012.