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 apr 2020
Accepted
21 mei 2020
First published
27 mei 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

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements