Issue 17, 2022

Nanobodies as solubilization chaperones for the expression and purification of inclusion-body prone proteins

Abstract

Here, we report a new protocol for enhancing the soluble expression of inclusion body (IB)-prone proteins in E. coli using nanobodies (Nbs) as a molecular-specific chaperone. The specific intracellular binding between the cognate-Nbs and the antigen is successfully achieved and enables the formation of a soluble Nb–antigen complex in E. coli. We further expand this method by adding an epitope tag (EPEA-tag) to the target proteins, and the anti-EPEA Nb was intended to act as the chaperone for in vivo binding with the EPEA tag. Such substitution may develop a “multi-specific” Nb-chaperone that can simultaneously and effectively cope with different IB proteins of interest.

Graphical abstract: Nanobodies as solubilization chaperones for the expression and purification of inclusion-body prone proteins

Supplementary files

Article information

Article type
Communication
Submitted
18 Dec 2021
Accepted
25 Jan 2022
First published
26 Jan 2022

Chem. Commun., 2022,58, 2898-2901

Nanobodies as solubilization chaperones for the expression and purification of inclusion-body prone proteins

G. Yao, C. Huang, F. Ji, J. Ren, X. Luo, B. Zang and L. Jia, Chem. Commun., 2022, 58, 2898 DOI: 10.1039/D1CC07105J

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