Sequence-specific inhibition of a designed metallopeptide catalyst.
Rhodium metallopeptides catalyze proximity-driven modification of peptide and protein substrates with enzyme-like selectivity. In this communication, we demonstrate that designed metallopeptide catalysts can be inhibited in a sequence-specific manner, mimicking the inhibition and regulation of natural enzymes. We demonstrate sub-micromolar inhibition by a histidine-containing inhibitor peptide, taking advantage of cooperative supramolecular assembly and inorganic coordination.
Department of Chemistry MS60, Rice University, 6100 Main St, Houston, TX 77005, USA.
Brian V
BV
Popp
Zhen
Z
Chen
Zachary T
ZT
Ball
D000595:Amino Acid Sequence; D055162:Biocatalysis; D040761:Biomimetic Materials / Q000737:chemistry*; D002384:Catalysis; D006639:Histidine / Q000737:chemistry; D008667:Metalloproteins / Q000737:chemistry; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D012238:Rhodium / Q000737:chemistry*
D008667:Metalloproteins; D010455:Peptides; D006639:Histidine; D012238:Rhodium