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Title: Polyoxometalates as novel class of artificial proteases: Insights by multinuclear NMR spectroscopy
Authors: Stroobants, Karen
Moelants, Eva
Ly Thi, Hong Giang
Proost, Paul
Absillis, Gregory
Parac-Vogt, Tatjana
Issue Date: Nov-2012
Conference: YBMRS 2012 edition:11 location:Spa date:26-27 November 2012
Abstract: As the known part of the protein universe keeps on growing, the scientific community has its hands full with unravelling the structure and function of this class of important biomolecules. Due to their large size, hydrolysis of proteins into more manageable and analyzable fragments is a frequently required procedure in the quest for structure and function elucidation. The natural enzymes and chemical agents that are currently used for protein hydrolysis in biochemical and biomedical practice have several drawbacks and only few of them are selective. This has inspired many research groups to design new artificial cleavage agents, with a recent focus on metal-containing complexes.1 Our research group combines the use of hydrolytic active metal ions with polyoxometalate (POM) ligands, which are known to specifically interact with proteins.2 Different POMs containing Lewis acidic metal ions were synthesized and characterized with 31P NMR spectroscopy. Both dipeptides and proteins were successfully hydrolyzed at pH 7.4 and 37 to 60 °C. In the case of dipeptide targets, the reactions were followed with 1H NMR spectroscopy in order to obtain full kinetic profiles of the reactions.3-5 Cleavage sites in larger protein targets were determined with SDS-PAGE and subsequent Edman degradation and the interaction at the respective sites was further studied with 31P NMR and 1H, 15N-HSQC NMR spectroscopy. The combination of multinuclear NMR experiments with SDS-PAGE, Edman degradation and CD spectroscopy experiments will result in a structure-function relationship of POMs as a new class of tunable artificial proteases.
Publication status: published
KU Leuven publication type: AMa
Appears in Collections:Molecular Design and Synthesis
Laboratory of Molecular Immunology (Rega Institute)

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