Enabling the study of protein glycosylation

Our interests include the study of protein glycosylation. In order to improve data acquisition during glycoproteomic studies, human Fbs1 protein was engineered for improved binding and enrichment of N-linked glycopeptides from complex biological samples.

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(C)

(A) Fluorescently-labeled (TMR) substrates designed to demonstrate N-glycopeptide binding properties of wt-Fbs1 and Fbs1-GYR.
(B) Fbs1-GYR exhibits unbiased binding of complex N-glycopeptides.
(C) Fbs1-GYR enables significant enrichment of intact N-glycopeptides from complex biological samples.

 

Minyong Chen, Xiaofeng Shi, Rebecca M. Duke, Cristian I. Ruse, Nan Dai, Christopher H. Taron & James C. Samuelson. (2017) An engineered high affinity Fbs1 carbohydrate binding protein for selective capture of N-glycans and N-glycopeptides. Nat. Commun. PMID: 28534482.

Minyong Chen, Steven J. Dupard, Colleen M. McClung, Cristian I. Ruse, Mehul B. Ganatra, Saulius Vainauskas, Christopher H. Taron and James C. Samuelson. (2021) Improving the Study of Protein Glycosylation with New Tools for Glycopeptide Enrichment. Book chapter, Fundamentals of Glycosylation DOI: 10.5772/intechopen.97339.