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.
Sambasivan
Ramya
R
Department of Chemistry, Rice University, MS 60, 6100 Main Street, Houston, Texas, USA.
Ball
Zachary T
ZT
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