Conjugate of palladium(II) complex and beta-cyclodextrin acts as a biomimetic peptidase.
We combined the newly discovered ability of [Pd(H2O)4]2+ to residue-selectively hydrolyze X-Pro bonds in peptides at 6 </= pH </= 9 with the known ability of beta-cyclodextrin to recognize aromatic side chains and synthesized a conjugate reagent that acts as a sequence-specific peptidase. This new reagent cleaved the Ser6-Pro7 amide bond in bradykinin at pH 7. ROESY 1H NMR spectra gave evidence for inclusion of the side chain of Phe8 in the beta-cyclodextrin cavity, the interaction that makes the cleavage sequence specific.
Milović
Nebojsa M
NM
Department of Chemistry, Gilman Hall, Iowa State University, Ames, Iowa 50011-3111, USA.
Badjić
Jovica D
JD
Kostić
Nenad M
NM
D040761:Biomimetic Materials / Q000737:chemistry* / Q000378:metabolism; D003505:Cyclodextrins / Q000737:chemistry* / Q000378:metabolism; D019906:Nuclear Magnetic Resonance, Biomolecular; D009842:Oligopeptides / Q000737:chemistry / Q000378:metabolism; D009942:Organometallic Compounds / Q000737:chemistry / Q000378:metabolism; D010165:Palladium / Q000737:chemistry*; D010447:Peptide Hydrolases / Q000737:chemistry* / Q000378:metabolism; D047392:beta-Cyclodextrins
D003505:Cyclodextrins; D009842:Oligopeptides; D009942:Organometallic Compounds; D047392:beta-Cyclodextrins; D010165:Palladium; D010447:Peptide Hydrolases; C031215:betadex