4.2 Review

Sialidase substrates for Sialdiase assays-activity, specificity, quantification and inhibition

期刊

GLYCOCONJUGATE JOURNAL
卷 37, 期 5, 页码 513-531

出版社

SPRINGER
DOI: 10.1007/s10719-020-09940-0

关键词

Desialylation; Neuraminidase; Sialic acid; Sialidase; sialylation; Chromophore; fluorophore and chemiluminescent substrate

资金

  1. Faculty Research Fund from the Center for Gene Regulation in Health and Disease (GRHD)
  2. Faculty Research Development (FRD) Fund
  3. Cleveland State University
  4. China Scholarship Council

向作者/读者索取更多资源

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.

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