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锆(IV)取代多金属氧酸盐促进天冬氨酸残基对肌红蛋白的高氨基酸选择性水解。

Highly Amino Acid Selective Hydrolysis of Myoglobin at Aspartate Residues as Promoted by Zirconium(IV)-Substituted Polyoxometalates.

机构信息

Department of Chemistry, KU Leuven, Celestijnenlaan 200F, 3001 Leuven (Belgium) http://www.chem.kuleuven.be/lbc/index.html.

Laboratory of Molecular Immunology, Rega Institute, Department of Microbiology and Immunology, KU Leuven, Minderbroedersstraat 10, 3000 Leuven (Belgium).

出版信息

Angew Chem Int Ed Engl. 2015 Jun 15;54(25):7391-4. doi: 10.1002/anie.201502006. Epub 2015 May 7.

DOI:10.1002/anie.201502006
PMID:25950869
Abstract

SDS-PAGE/Edman degradation and HPLC MS/MS showed that zirconium(IV)-substituted Lindqvist-, Keggin-, and Wells-Dawson-type polyoxometalates (POMs) selectively hydrolyze the protein myoglobin at Asp-X peptide bonds under mildly acidic and neutral conditions. This transformation is the first example of highly sequence selective protein hydrolysis by POMs, a novel class of protein-hydrolyzing agents. The selectivity is directed by Asp residues located on the surface of the protein and is further assisted by electrostatic interactions between the negatively charged POMs and positively charged surface patches in the vicinity of the cleavage site.

摘要

SDS-PAGE/Edman 降解和 HPLC-MS/MS 表明,锆(IV)取代的 Lindqvist、Keggin 和 Wells-Dawson 型多金属氧酸盐(POM)在弱酸和中性条件下选择性地水解蛋白质肌红蛋白中的 Asp-X 肽键。这种转化是 POM 对蛋白质进行高度序列选择性水解的首例,POM 是一类新型的蛋白质水解试剂。这种选择性是由位于蛋白质表面的 Asp 残基决定的,并通过带负电荷的 POM 与靠近切割位点的带正电荷的表面斑块之间的静电相互作用得到进一步辅助。

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