Metallopeptides for asymmetric dirhodium catalysis.
Natural peptide sequences ligate to dirhodium centers through two bridging aspartate side chains, creating a macromolecular ligand framework with helical structure. The generation of a small peptide library allowed optimization of peptide sequence and produced an efficient catalyst for enantioselective carbenoid insertion into Si-H bonds. Analysis of the library indicates that the i-1 and i+3 positions of nonapeptides have the most significant effect on enantioselectivity, though the structural basis for selectivity is different at each of the positions.
Department of Chemistry, Rice University, MS 60, 6100 Main Street, Houston, Texas, USA.
Ramya
R
Sambasivan
Zachary T
ZT
Ball
D000595:Amino Acid Sequence; D001224:Aspartic Acid; D002384:Catalysis; D008024:Ligands; D008670:Metals / Q000737:chemistry*; D008968:Molecular Conformation; D009842:Oligopeptides / Q000737:chemistry*; D019151:Peptide Library; D012238:Rhodium / Q000737:chemistry*; D012825:Silicon
D008024:Ligands; D008670:Metals; D009842:Oligopeptides; D019151:Peptide Library; D001224:Aspartic Acid; D012238:Rhodium; D012825:Silicon