Sialidase substrates for Sialdiase assays - activity, specificity, quantification and inhibition
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REVIEW ARTICLE
Sialidase substrates for Sialdiase assays - activity, specificity, quantification and inhibition Lei Yuan 1,2 & Yu Zhao 1 & Xue-Long Sun 1 Received: 28 May 2020 / Revised: 8 July 2020 / Accepted: 6 August 2020 # Springer Science+Business Media, LLC, part of Springer Nature 2020
Abstract Sialidases are glycosidases responsible for the removal of sialic acid (Sia) residues (desialylation) from glycan portions of either glycoproteins or glycolipids. By desialylation, sialidases are able to modulate the functionality and stability of the Sia-containing molecules and are involved in both physiological and pathological pathways. Therefore, evaluation of sialidase activity and specificity is important for understanding the biological significance of desialylation by sialidases and its function and the related molecular mechanisms of the physiological and pathological pathways. In addition, it is essential for developing novel mechanisms and approaches for disease treatment and diagnosis and pathogen detection as well. This review summarizes the most recent sialidase substrates for evaluating sialidase activity and specificity and screening sialidase inhibitors, including (i) general sialidase substrates, (ii) specific sialidase substrates, (iii) native sialidase substrates and (iv) cellular sialidase substrates. This review also provides a brief introduction of recent instrumental methods for quantifying the sialidase activity, such as UV, fluorescence, HPLC and LC-MS methods. Keywords Desialylation . Neuraminidase . Sialic acid . Sialidase, sialylation . Chromophore, fluorophore and chemiluminescent substrate
Abbreviation 4MU 4TFMUNeu5Ac 4MU-9-OAc-Neu5Ac 4MU-9O-Ac-Neu5Gc Az BODIPY BV
4-methylumbelliferone 4-trifluoromethylumbelliferylα-D-N-acetylneuraminic acid 2′-(4-methylumbelliferyl)9-O-acetyl-α-D-N-acetylneuraminic acid 2′-(4-methylumbelliferyl)-9O-acetyl-α-D-N-glycolylneuraminic acid azidoacetyl Boron-dipyrromethene bacterial vaginosis
Sialidase Substrates – From Sialosides, Sialylglycoconjugates to Cellular Sialylation with Un-nature Sialic Acids * Xue-Long Sun [email protected] 1
Department of Chemistry, Chemical and Biomedical Engineering and Center for Gene Regulation in Health and Disease (GRHD), Cleveland State University, 2121 Euclid Avenue, Cleveland, OH 44115, USA
2
School of Pharmaceutical Engineering, Shenyang Pharmaceutical University, Shenyang 110016, People’s Republic of China
DFSAs DMB DPPC DPPE DPPS ELLA Gal GalNAc GM1 GM3 HPLC IDMS LC-MS ManNR MGE NAs NEU NI p-NP-Neu5Ac
2,3-difluoro-sialic acids 4,5-methylenedioxy-1, 2-phenylenediamine dipalmitoyl phosphatidylcholine dipalmitoyl phosphatidylethanolamine dipalmitoyl phosphatidylserine enzyme-linked lectin assay galactose N-acetyl galactosamine monosialotetrahexosylganglioside 1 monosialotetrahexosylganglioside 3 high performance liquid chromatography isotope dilution mass spectrometry Liquid chromatography– mass spectrometry mannosamine derivatives Metabolic glycoengineering Sialidases or Neuraminidases Neuraminidase virus
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