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Functionalization of protein hexahistidine tags by functional nanoreactors.
- Source :
-
New Journal of Chemistry . 12/14/2019, Vol. 43 Issue 46, p17946-17953. 8p. - Publication Year :
- 2019
-
Abstract
- A water-soluble Morita–Baylis–Hillman adduct (MBHA) derivative (3) was previously shown to self-assemble in a water environment into functional nanoreactors capable of performing multiple attacks and functionalization of N-acetylhexahistidine. In order to challenge this intriguing reactivity in a model protein more complex than N-acetylhexahistidine, the single-chain Fv antibody CRB0137 was characterized from the point of view of its structure and made to react with 3 in kinetics experiments. The results of these studies suggested that MBHA derivative 3 reacted typically with the amino acid residues of the CRB0137 hexahistidine tag leading to the formation of multi-PEGylated species. Overall, they demonstrate the viability of a new methodology for the site-specific PEGylation of engineered proteins bearing poly-histidine tags. [ABSTRACT FROM AUTHOR]
- Subjects :
- *HISTIDINE
*AMINO acid residues
*PROTEINS
*PROTEIN models
Subjects
Details
- Language :
- English
- ISSN :
- 11440546
- Volume :
- 43
- Issue :
- 46
- Database :
- Academic Search Index
- Journal :
- New Journal of Chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 139870605
- Full Text :
- https://doi.org/10.1039/c9nj03463c