Accurate Quantification of N-Glycolylneuraminic Acid in Therapeutic Proteins Using Supramolecular Mass Spectrometry

Citations

WEB OF SCIENCE

13
Citations

SCOPUS

13

초록

Practical applications of innovative host-guest systems are challenging because of unexpected guest competitors and/or subtle environmental differences. Herein, a supramolecular mass spectrometry (MS)-based method using a synthetic host, cucurbit[7]uril (CB[7]), was developed for identifying and quantifying N-glycolylneuraminic acid (Neu5Gc) in therapeutic glycoproteins, which critically reduces drug efficacy. The development of a reliable derivatization-free analytical method for Neu5Gc is highly challenging because of the interference by the abundant N-acetylneuraminic acid (Neu5Ac). CB[7] recognized the subtle structural differences between Neu5Gc and Neu5Ac. Distinct host-guest interactions between CB[7] and the two sialic acids produced a highly linear relationship between the complexation and concentration proportions of the two sialic acids in MS. Furthermore, the developed method had sub-picomolar quantification limits and a wide range of applicability for diverse glycoproteins, demonstrating the potential utility of this method as a reliable assay of Neu5Gc in therapeutic glycoproteins.

키워드

ANION-EXCHANGE CHROMATOGRAPHY; PERFORMANCE LIQUID-CHROMATOGRAPHY; SIALIC ACIDS; PHASE; MICRODETERMINATION; GLYCOPROTEINS; PROTONATION; ALGORITHMS; CHEMISTRY; BINDING
제목
Accurate Quantification of N-Glycolylneuraminic Acid in Therapeutic Proteins Using Supramolecular Mass Spectrometry
저자
Lee, Hyun Hee L.; Heo, Chae Eun; Seo, Nari; Yung, Seung Gyu; An, Hyun Joo; Kim, Hugh, I
DOI
10.1021/jacs.8b07864
발행일
2018-12
유형
Article
저널명
Journal of the American Chemical Society
권
140
호
48
페이지
16528 ~ 16534