Disulphide-mediated site-directed modification of proteins
| Autor: | Milan Štengl, Emiliano Cló, Zuzana Drobňáková, Anders Märcher, Vojtěch Balšánek, Thomas E. Nielsen, Michal Hučko, Per Franklin Nielsen, Thorbjørn B. Nielsen, Charlotte Wiberg, Kurt V. Gothelf |
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| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
chemistry.chemical_classification
Molecular Structure Chemistry Lysine Human growth hormone Organic Chemistry Chemical modification Biochemistry Combinatorial chemistry Solvent chemistry.chemical_compound Growth Hormone Reagent Thiol Side chain Humans Disulfides Physical and Theoretical Chemistry Bifunctional |
| Zdroj: | Nielsen, T, Märcher, A, Drobňáková, Z, Hučko, M, Štengl, M, Balšánek, V, Wiberg, C, Nielsen, P F, Nielsen, T E, Gothelf, K V & Cló, E 2020, ' Disulphide-mediated site-directed modification of proteins ', Organic and Biomolecular Chemistry, vol. 18, no. 25, pp. 4717-4722 . https://doi.org/10.1039/d0ob00861c |
| DOI: | 10.1039/d0ob00861c |
| Popis: | 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. This journal is |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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