Analyzing glycans cleaved from a biotherapeutic protein using ultrahigh-resolution ion mobility spectrometry together with cryogenic ion spectroscopy. Issue 20 (4th August 2020)

• Record Type: Journal Article
• Authors: Yalovenko, Natalia; Yatsyna, Vasyl; Bansal, Priyanka; AbiKhodr, Ali H.; Rizzo, Thomas R.
• Is Part Of: Analyst. Volume 145:Issue 20(2020)
• Page Start: 6493
• Page End: 6499
• Publication Date: 2020-08-04
• Subjects: Chemistry, Analytic -- Periodicals; 543
• DOI: 10.1039/d0an01206h
• Languages: English
• ISSNs: 0003-2654

Abstract

Abstract : A new approach for analysis of cleaved glycans. Abstract : Glycans covalently attached to protein biotherapeutics have a significant impact on their biological activity, clearance, and safety. As a result, glycosylation is categorized as a critical quality attribute that needs an adequate analytical approach to guarantee product quality. However, the isomeric complexity and branched structure of glycans makes their analysis a significant challenge. In this work, we propose a multidimensional approach for monitoring released glycans that combines ultrahigh-resolution ion mobility spectrometry (IMS) and cryogenic vibrational spectroscopy, and we demonstrate this technique by characterizing four N -glycans cleaved from the therapeutic fusion protein etanercept that range in abundance from 1% to 22% of the total N -glycan content. The recorded vibrational spectra exhibit well-resolved transitions that can be used as a fingerprint to identify a particular glycan. This work represents an important advance in the analysis of N-linked glycans cleaved from biopharmaceutical proteins that could eventually be used as tool for monitoring biopharmaceutical glycoforms.