A novel approach to the site-selective dual labelling of a protein via chemoselective cysteine modification

Local protein microenvironment is used to control the outcome of reaction between cysteine residues and 2,5-dibromohexanediamide. The differential reactivity is exploited to introduce two orthogonal reactive handles onto the surface of a double cysteine mutant of superfolder green fluorescent protei...

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Detalles Bibliográficos
Autores principales: Nathani, Ramiz I., Moody, Paul, Chudasama, Vijay, Smith, Mark E. B., Fitzmaurice, Richard J., Caddick, Stephen
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Royal Society of Chemistry 2013
Materias:
Chemistry
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3985185/
https://www.ncbi.nlm.nih.gov/pubmed/24741436
http://dx.doi.org/10.1039/c3sc51333e
Descripción
Sumario:Local protein microenvironment is used to control the outcome of reaction between cysteine residues and 2,5-dibromohexanediamide. The differential reactivity is exploited to introduce two orthogonal reactive handles onto the surface of a double cysteine mutant of superfolder green fluorescent protein in a regioselective manner. Subsequent elaboration with commonly used thiol and alkyne containing reagents affects site-selective protein dual labelling.

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