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 allo...

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Bibliographic Details
Published in:Journal of the American Chemical Society 2004-06, Vol.126 (22), p.6967-6971
Main Authors: Fierman, Matthew B, O'Leary, Daniel J, Steinmetz, Wayne E, Miller, Scott J
Format: Article
Language:English
Subjects:
Acylation
Catalysis
Chemical reactivity
Chemistry
Exact sciences and technology
Kinetics
Models, Molecular
Molecular Structure
Nuclear Magnetic Resonance, Biomolecular
Organic chemistry
Peptides - chemistry
Peptides - metabolism
Protein Conformation
Reactivity and mechanisms
Stereoisomerism
Structure-Activity Relationship
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Summary: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.
ISSN:0002-7863
1520-5126
DOI:10.1021/ja049661c