Gruber, Tobias (2018) Synthetic receptors for the recognition and discrimination of post-translationally methylated lysines. ChemBioChem, 19 (22). pp. 2324-2340. ISSN 1439-4227
Full content URL: https://doi.org/10.1002/cbic.201800398
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Item Type: | Article |
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Item Status: | Live Archive |
Abstract
Post-translational modifications (PTMs) describe the chemical alteration of proteins after their biosynthesis in ribosomes. PTMs play important roles in cell biology including the regulation of gene expression, cell-cell interactions and the development of different diseases. A prominent class of PTMs is the side chain methylation of lysine. For the analysis and discrimination of differently methylated lysines antibodies are widely used, though, methylated peptide and protein targets are known to be particularly difficult to be differentiated by antibody-based affinity reagents; an additional challenge can be batch-to-batch reproducibility. The application of mass spectrometry techniques for methyllysine discrimination requires a complex sample preparation and is not suited for working in cells. The desire to overcome above-named challenges promoted the development of synthetic receptor molecules that recognize and bind methyllysines. Such ‘artificial antibodies’ are of interest for a number of applications, e.g. as reagents in biochemical assays, for the isolation and purification of post-translationally methylated proteins and for the tracking of signalling pathways. Moreover, they offer new approaches in diagnostics and therapy. This review delivers an overview of the broad field of methyllysine binding and covers a wide range of synthetic receptors used for the recognition of methylated lysines including calixarenes, resorcinarenes, pillararenes, disulfide cyclophanes, cucurbituriles and acyclic receptors.
Additional Information: | © 2018 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim |
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Keywords: | Post-translational modification, Lysine methylation, Artificial antibodies, Synthetic receptors, Epigenetics |
Subjects: | B Subjects allied to Medicine > B230 Pharmacy F Physical Sciences > F150 Medicinal Chemistry F Physical Sciences > F151 Pharmaceutical Chemistry |
Divisions: | College of Science > School of Pharmacy |
ID Code: | 33048 |
Deposited On: | 28 Aug 2018 14:09 |
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