Issue 25, 2020

Disulphide-mediated site-directed modification of proteins

Abstract

Methods for chemical modification of native proteins in a controlled fashion are in high demand. Here, a novel protocol that exploits bifunctional reagents for transient targeting of solvent exposed disulphides to direct the introduction of a single exogenous reactive thiol handle at a lysine side chain has been developed. The protocol has successfully been applied to functionalize six different Fabs and human growth hormone.

Graphical abstract: Disulphide-mediated site-directed modification of proteins

Supplementary files

Article information

Article type
Communication
Submitted
24 4 2020
Accepted
21 5 2020
First published
27 5 2020

Org. Biomol. Chem., 2020,18, 4717-4722

Disulphide-mediated site-directed modification of proteins

T. Nielsen, A. Märcher, Z. Drobňáková, M. Hučko, M. Štengl, V. Balšánek, C. Wiberg, P. F. Nielsen, T. E. Nielsen, K. V. Gothelf and E. Cló, Org. Biomol. Chem., 2020, 18, 4717 DOI: 10.1039/D0OB00861C

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