A Glycal-Based Photoaffinity Probe That Enriches Sialic Acid Binding Proteins

18 July 2019, Version 1
This content is a preprint and has not undergone peer review at the time of posting.

Abstract

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 7to 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.

Keywords

sialic acid
Activity-based probe
sialidase inhibitors
lectin
neu5ac

Supplementary materials

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Thuy-Boun 2019 SI chemrxiv
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Thuy-Boun 2019 SI data chemrxiv
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