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Bài báo - Tạp chí
(2012) Trang:
Tạp chí: Chemistry conference for young scientists 2012 - ChemCYS2012, Blankenberge, Belgium 1-2 March 2012
Liên kết:

Selective cleavage of peptides and proteins is one of the most important procedures in analytical biochemistry.  However, the extreme inertness of the amide bond with a half-life estimated to be up to 600 years under the physiological pH and temperature makes this task highly challenging. Several proteolytic enzymes are available, but they are usually not regioselective and cleave proteins in short fragments which are difficult to identify. Few existing synthetic reagents require harsh conditions and even when applied in great excess over the substrate, they tend to cleave proteins with partial selectivity and low yields. Metal-substituted polyoxometalates (POMs) have been developed as promising reagents for the hydrolysis of the amide bond. By using monolacunary Lindqvist anions [W5O18]6- as ligands for Zr(IV) ion, we have created a novel approach for selective and efficient peptide hydrolysis. With the highly negative charge, strong Lewis acid, oxophilicity and redox inactivity, Zirconium(IV)-substituted Lindqvist-Type Polyoxometalate is able to selectively interact with positively charged dipeptides as well as positive protein regions. In this paper, the hydrolysis of various dipeptides was studied in the presence of the complex (Me4N)2[W5O18Zr(H2O)3] by 1H and 13C NMR spectroscopy. The molecular mechanism of the peptide bond cleavage has also been elucidated from detailed kinetic experiments.

Các bài báo khác
Số 10 (2008) Trang: 41-50
Tải về
(2013) Trang: 28
Tạp chí: Young Belgium Magnetic Resonance Scientist 2013, 2nd-3rd December 2013, Blankenberge - Belgium
(2013) Trang:
Tạp chí: XIVth International Conference on Biological Inorganic Chemistry, Grenoble-France 22-27 July 2013
(2012) Trang:
Tạp chí: Young Belgian Magnetic Resonance Scientist Symposium YBNMRS 2012 - Spa, Belgium 26-27 November 2012

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