Selectivity and stability of N-terminal targeting protein modification chemistries. Issue 1 (22nd November 2022)

• Record Type: Journal Article
• Authors: Barber, Lydia J.; Yates, Nicholas D. J.; Fascione, Martin A.; Parkin, Alison; Hemsworth, Glyn R.; Genever, Paul G.; Spicer, Christopher D.
• Is Part Of: RSC chemical biology. Volume 4:Issue 1(2023)
• Page Start: 56
• Page End: 64
• Publication Date: 2022-11-22
• Subjects: 572
• DOI: 10.1039/d2cb00203e
• Languages: English
• ISSNs: 2633-0679

Abstract

Abstract : Protein N-termini provide uniquely reactive motifs for single site protein modification. A comprehensive comparative study of the most promising modification reagents is performed, finding that there is no 'one size fits all' approach. Abstract : Protein N-termini provide uniquely reactive motifs for single site protein modification. Though a number of reactions have been developed to target this site, the selectivity, generality, and stability of the conjugates formed has not been studied. We have therefore undertaken a comprehensive comparative study of the most promising methods for N-terminal protein modification, and find that there is no 'one size fits all' approach, necessitating reagent screening for a particular protein or application. Moreover, we observed limited stability in all cases, leading to a need for continued innovation and development in the bioconjugation field.