Issue 89, 2022

Residue-specific N-terminal glycine to aldehyde transformation renders analytically pure single-site labeled proteins

Abstract

Here, we present N-Gly-specific glyoxamide generation in native proteins, isolated or in a complex mixture. The resulting aldehyde enables parallel installation of probes and a purification platform to render analytically pure single-site tagged proteins. It renders N-Gly engineered insulin without perturbing its structure, receptor binding, and downstream signaling pathway.

Graphical abstract: Residue-specific N-terminal glycine to aldehyde transformation renders analytically pure single-site labeled proteins

Supplementary files

Article information

Article type
Communication
Submitted
28 ذو الحجة 1443
Accepted
17 ربيع الأول 1444
First published
21 ربيع الأول 1444

Chem. Commun., 2022,58, 12451-12454

Residue-specific N-terminal glycine to aldehyde transformation renders analytically pure single-site labeled proteins

T. Sahu, M. Kumar, S. T. K., M. Joshi, R. K. Mishra and V. Rai, Chem. Commun., 2022, 58, 12451 DOI: 10.1039/D2CC04196K

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