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Bài báo - Tạp chí
(2013) Trang:
Tạp chí: XIVth International Conference on Biological Inorganic Chemistry, Grenoble-France 22-27 July 2013
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 at 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. The 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. In the search for new artificial peptidases, metal-substituted polyoxometalates (POMs) have been intensively investigated in our research group for the hydrolysis of peptide bonds in peptides.[1] In this study, Zr(IV) was incorporated into monolacunary Keggin anions [PW11O39]7- to form a dimeric 2:2 Zr(IV)-substituted Keggin type POM, (Et2NH2)8[{?-PW11O39Zr(à-OH)(H2O)}2]?7H2O  (1). The stability of the POM is highly dependent on pH and its concentration, and can be monitored by 31P NMR spectroscopy. Various Gly-X and X-Gly dipeptides were proven to be effectively hydrolyzed by 1 and their hydrolysis was highly dependent on the nature of the side chain. The molecular mechanism of the peptide bond cleavage was elucidated based on combination of detailed kinetic experiments and multinuclear 1H, 13C and 31P NMR spectroscopy.

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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
(2012) Trang:
Tạp chí: Chemistry conference for young scientists 2012 - ChemCYS2012, Blankenberge, Belgium 1-2 March 2012
(2012) Trang:
Tạp chí: Young Belgian Magnetic Resonance Scientist Symposium YBNMRS 2012 - Spa, Belgium 26-27 November 2012

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