Studies of folded peptide-based catalysts for asymmetric organic synthesis.
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.
Blank
Jarred T
JT
Department of Chemistry, Merkert Chemistry Center, Boston College, Chestnut Hill, MA 02467-3860, USA.
Miller
Scott J
SJ
D000215:Acylation; D002384:Catalysis; D018360:Crystallography, X-Ray; D009682:Magnetic Resonance Spectroscopy; D015394:Molecular Structure; D009930:Organic Chemicals / Q000138:chemical synthesis*; D010455:Peptides / Q000737:chemistry*; D010766:Phosphorylation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D013237:Stereoisomerism
D009930:Organic Chemicals; D010455:Peptides