Selective Hydrolysis of Ovalbumin Promoted by Hf(IV)-Substituted Wells-Dawson-Type Polyoxometalate.

ABSTRACT: The reactivity and selectivity of Wells-Dawson type polyoxometalate (POM), K₁₆[Hf(α₂-P₂W₁₇O₆₁)₂]·19H₂O (Hf1-WD2), have been examined with respect to the hydrolysis of ovalbumin (OVA), a storage protein consisting of 385 amino acids. The exact cleavage sites have been determined by Edman degradation experiments, which indicated that Hf1-WD2 POM selectively cleaved OVA at eight peptide bonds: Phe13-Asp14, Arg85-Asp86, Asn95-Asp96, Ala139-Asp140, Ser148-Trp149, Ala361-Asp362, Asp362-His363, and Pro364-Phe365. A combination of spectroscopic methods including ³¹P NMR, Circular Dichroism (CD), and Tryptophan (Trp) fluorescence spectroscopy were employed to gain better understanding of the observed selective c

SUBMITTER: Anyushin AV 

PROVIDER: S-EPMC6305993 | biostudies-literature | 2018

REPOSITORIES: biostudies-literature