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

  • Cleveland State University
  • Shenyang Pharmaceutical University

Research output: Contribution to journalReview articlepeer-review

11 Scopus citations

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.
Original languageEnglish
Pages (from-to)513-531
Number of pages19
JournalGlycoconjugate Journal
Volume37
Issue number5
DOIs
StatePublished - Oct 1 2020

Keywords

  • Chromophore, fluorophore and chemiluminescent substrate
  • Desialylation
  • Neuraminidase
  • Sialic acid
  • Sialidase, sialylation

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