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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.
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Milović et al. (2003) studied this question.
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