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Publication

Development of metal-oxo clusters as homogeneous and heterogeneous artificial proteases

Book - Dissertation

Proteomics studies the complete set of proteins found in living cells, tissues or organisms, representing the end result of gene transcription, translation, and protein synthesis up to post-translational protein modifications (PTM). As proteins are key players in biochemical and biological processes the study of protein levels, function, localization, and regulation is of crucial importance in biological and biomedicinal research. Generally, most proteomics approaches rely on protein digestion to produce easily analysable protein fragments, commonly generated by proteases. Overall, the most used protease is trypsin, due to it high efficiency, reasonably low cost and ease of analysis. However, roughly 50 % of the tryptic peptides are too short to be nicely fragmented and uniquely assigned to a protein, which has led to a restricted view of the analysed sequences. Therefore, new cleavage agents could provide interesting alternatives by introducing different cleavage selectivity. Based on nature's example of the presence of metals in the active site of metalloproteases, metals and their complexes have been extensively studied as artificial proteases for amide bond hydrolysis. An excellent group of candidates are metal-oxo clusters, a vast class of compounds spanning organic and inorganic fields with examples such as metal-organic frameworks, discrete metal-oxo clusters and metal-substituted polyoxometalates. The large variety of clusters possess attractive physicochemical properties that have seen use in a wide diversity of fields such as catalysis, electronics, medicine,… While the performance of metal-substituted polyoxometalates has been established in recent years, other metal-oxo clusters have scarcely been explored as artificial proteases. Therefore, in this thesis we aim to broaden the scope of the vast group of metal-oxo clusters as artificial proteases for proteomics applications. Moreover, we aim to further establish the advantage of using metal-substituted polyoxometalates in proteomics.
Publication year:2021
Accessibility:Closed