Novel Cleavage of Reductively Aminated Glycan-Tags by N-Bromosuccinimide to Regenerate Free, Reducing Glycans

• Type of Material: Article
• Authors: Xuezheng Song, Emory University; Brian A. Johns, Emory University; Hong Ju, Emory University; Yi Lasanajak, Emory University; Chunmei Zhao, Emory University; David Smith, Emory University; Richard Cummings, Emory University
• Language: English
• Date: 2013-11-01
• Publisher: American Chemical Society
• Publication Version: Author Accepted Manuscript (After Peer Review)
• Copyright Statement: © 2013 American Chemical Society.
• Final Published Version (URL): http://dx.doi.org/10.1021/cb400513k
• Title of Journal or Parent Work: ACS Chemical Biology
• ISSN: 1554-8929
• Volume: 8
• Issue: 11
• Start Page: 2478
• End Page: 2483
• Grant/Funding Information: This work was supported by a EUREKA Grant (GM085448) (to D.F.S); and a Defense Advanced Research Projects Agency Grant HR0011-10-00; and P41 BTRC grant (P41GM10369) (to R.D.C).
• Keywords: FLUORESCENT COMPOUND; END; DERIVATIVES; MICROARRAY STRATEGY; Biochemistry & Molecular Biology; Science & Technology; OLIGOSACCHARIDES; FUNCTIONAL GLYCOMICS; Life Sciences & Biomedicine; SUGARS
• Research Categories: Chemistry, Biochemistry

Abstract

Glycans that are fluorescently tagged by reductive amination have been useful for functional glycomic studies. However, the existing tags can introduce unwanted properties to the glycans and complicate structural and functional studies. Here, we describe a facile method using N-bromosuccinimide (NBS) to remove the tags and efficiently regenerate free reducing glycans. The regenerated free reducing glycans can be easily analyzed by routine mass spectrometry or retagged with different tags for further studies. This new method can be used to efficiently remove a variety of fluorescent tags installed by reductive amination, including 2-aminobenzoic acid and 2-aminopyridine. NBS treatment essentially transforms the commonly used 2-aminobenzoic linkage to a cleavable linkage. It can be used to cleave printed glycans from microarrays and cleave neoglycopeptides containing a 2-aminobenzoic linker.