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Studies of folded peptide‐based catalysts for asymmetric organic synthesis
Author(s) -
Blank Jarred T.,
Miller Scott J.
Publication year - 2005
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.20392
Subject(s) - chemistry , peptide , rational design , combinatorial chemistry , catalysis , peptidomimetic , structural motif , nanotechnology , stereochemistry , computational biology , biochemistry , materials science , biology
Folded peptides have proven to be a fertile area for discovery of catalysts for reactions in organic synthesis. Both combinatorial chemistry and rational design have fueled these discoveries. In both lines of research, mechanistic studies following the discovery of selective reactions have led to structural information that has stimulated attempts to correlate peptide structure and the relay of stereochemical information. Thus, key elements of the design of peptide‐based catalysts include the identification of catalytically competent functional groups and their incorporation into three‐dimensional structures that provide an appropriate chiral environment. Of note, turns, helices, nonobvious folds, and still undetermined secondary structures characterize the structural and functionally diverse motifs that enable peptide‐catalyzed asymmetric reactions to occur. © 2005 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 84: 38–47, 2006 This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com