Milović Nebojsa M, Badjić Jovica D, Kostić Nenad M
Department of Chemistry, Gilman Hall, Iowa State University, Ames, Iowa 50011-3111, USA.
J Am Chem Soc. 2004 Jan 28;126(3):696-7. doi: 10.1021/ja038404p.
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.
我们将新发现的[Pd(H₂O)₄]²⁺在6≤pH≤9时对肽中X - Pro键进行残基选择性水解的能力与β - 环糊精识别芳香族侧链的已知能力相结合，合成了一种作为序列特异性肽酶的共轭试剂。这种新试剂在pH 7时可切割缓激肽中的Ser6 - Pro7酰胺键。ROESY ¹H NMR光谱证明了β - 环糊精腔中包含Phe8的侧链，这种相互作用使得切割具有序列特异性。
