Oxidative Folding of Proteins: Basic Principles, Cellular Regulation and Engineering
CHAPTER 1.4: Analysis of Disulfide Bond Formation in Therapeutic Proteins
Published:27 Jul 2018
Special Collection: 2018 ebook collectionSeries: Chemical Biology
D. Weinfurtner, in Oxidative Folding of Proteins: Basic Principles, Cellular Regulation and Engineering, ed. M. J. Feige, The Royal Society of Chemistry, 2018, pp. 81-98.
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Correct disulfide bond formation is a prerequisite for the structural integrity and biological activity of many proteins. Consequently, assessing a protein's native disulfide linkage pattern is of critical importance in understanding its structure–function relationship. The need to ensure efficacy and safety both in biological drug development and in academic research have helped to develop several analytical strategies to cope with this sometimes cumbersome task. Despite the availability of spectroscopic and electrophoretic methods, mass spectrometry-based analysis has become the predominant method used today. This chapter is intended to give researchers in all areas, academic and industry, a comprehensive overview of common degradation pathways of disulfide bonds and to serve as a starting point for setting up state-of-the art analytical methods to analyze the disulfide integrity and linkage patterns.