A glycal-based photoaffinity probe that enriches sialic acid binding proteins

Peter S. Thuy-Boun, Dennis W. Wolan

Research output: Contribution to journalArticlepeer-review

8 Scopus citations


To identify sialic acid binding proteins from complex proteomes, three photocrosslinking affinity-based probes were constructed using Neu5Ac (5 and 6) and Neu5Ac2en (7) scaffolds. Kinetic inhibition assays and Western blotting revealed the Neu5Ac2en-based 7 to be an effective probe for the labeling of a purified gut microbial sialidase (BDI_2946) and a purified human sialic acid binding protein (hCD33). Additionally, LC–MS/MS affinity-based protein profiling verified the ability of 7 to enrich a low-abundance sialic acid binding protein (complement factor H) from human serum thus validating the utility of this probe in a complex context.

Original languageEnglish
Pages (from-to)2609-2612
Number of pages4
JournalBioorganic and Medicinal Chemistry Letters
Issue number18
StatePublished - 15 Sep 2019
Externally publishedYes


  • Activity-based probe
  • Lectin
  • Neu5Ac
  • Sialic acid
  • Sialidase


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