Structure-selectivity relationships and structure for a peptide-based enantioselective acylation catalyst.
Studies of analogues of a recently discovered enantioselective peptide-based catalyst for enantioselective acylation reactions have led to mechanistic insight and improved catalysts. Systematic replacement of each residue within the parent peptide with alanine of the appropriate stereochemistry allows for an unambiguous evaluation of the kinetic role of each amino acid side chain in the catalyst. The results of the alanine scan support a bifunctional catalysis mechanism at the heart of the origin of enantioselectivity. In addition, an experimentally derived solution structure of the peptide-based catalyst is presented that supports a key role for each residue within the peptide chain.
Fierman
Matthew B
MB
Department of Chemistry, Merkert Chemistry Center, Boston College, Chestnut Hill, Massachusetts 02467-3860, USA.
O'Leary
Daniel J
DJ
Steinmetz
Wayne E
WE
Miller
Scott J
SJ
D000215:Acylation; D002384:Catalysis; D007700:Kinetics; D008958:Models, Molecular; D015394:Molecular Structure; D019906:Nuclear Magnetic Resonance, Biomolecular; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism*; D011487:Protein Conformation; D013237:Stereoisomerism; D013329:Structure-Activity Relationship
D010455:Peptides