Nanobodies as solubilization chaperones for the expression and purification of inclusion-body prone proteins. Issue 17 (9th February 2022)

• Record Type: Journal Article
• Authors: Yao, Guangshuai; Huang, Chundong; Ji, Fangling; Ren, Jun; Luo, Xiuna; Zang, Berlin; Jia, Lingyun
• Is Part Of: Chemical communications. Volume 58:Issue 17(2022)
• Page Start: 2898
• Page End: 2901
• Publication Date: 2022-02-09
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1039/d1cc07105j
• Languages: English
• ISSNs: 1359-7345

Abstract

Abstract : Nanobodies as molecular-specific chaperones assist in the folding of antigen proteins via specific binding in vivo. 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.