Optimisation of chemical protein cleavage for erythropoietin semi-synthesis using native chemical ligation

Selective protein cleavage at methionine residues is a useful method for the production of bacterially derived protein fragments containing an N-terminal cysteine residue required for native chemical ligation. Here we describe an optimised procedure for cyanogen bromide-mediated protein cleavage, an...

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Detalles Bibliográficos
Autores principales: Richardson, Jonathan P., Macmillan, Derek
Formato: Texto
Lenguaje:English
Publicado: Royal Society of Chemistry 2008
Materias:
Chemistry
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2898651/
https://www.ncbi.nlm.nih.gov/pubmed/18931805
http://dx.doi.org/10.1039/b811501j
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author Richardson, Jonathan P.
Macmillan, Derek
author_facet Richardson, Jonathan P.
Macmillan, Derek
author_sort Richardson, Jonathan P.
collection PubMed
description Selective protein cleavage at methionine residues is a useful method for the production of bacterially derived protein fragments containing an N-terminal cysteine residue required for native chemical ligation. Here we describe an optimised procedure for cyanogen bromide-mediated protein cleavage, and ligation of the resulting fragments to afford biologically active proteins.
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spelling pubmed-28986512011-09-26 Optimisation of chemical protein cleavage for erythropoietin semi-synthesis using native chemical ligation Richardson, Jonathan P. Macmillan, Derek Org Biomol Chem Chemistry Selective protein cleavage at methionine residues is a useful method for the production of bacterially derived protein fragments containing an N-terminal cysteine residue required for native chemical ligation. Here we describe an optimised procedure for cyanogen bromide-mediated protein cleavage, and ligation of the resulting fragments to afford biologically active proteins. Royal Society of Chemistry 2008-11-07 2008-09-05 /pmc/articles/PMC2898651/ /pubmed/18931805 http://dx.doi.org/10.1039/b811501j Text en This journal is © The Royal Society of Chemistry 2008 http://creativecommons.org/licenses/by-nc/2.0/uk/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Chemistry
Richardson, Jonathan P.
Macmillan, Derek
Optimisation of chemical protein cleavage for erythropoietin semi-synthesis using native chemical ligation
title Optimisation of chemical protein cleavage for erythropoietin semi-synthesis using native chemical ligation
title_full Optimisation of chemical protein cleavage for erythropoietin semi-synthesis using native chemical ligation
title_fullStr Optimisation of chemical protein cleavage for erythropoietin semi-synthesis using native chemical ligation
title_full_unstemmed Optimisation of chemical protein cleavage for erythropoietin semi-synthesis using native chemical ligation
title_short Optimisation of chemical protein cleavage for erythropoietin semi-synthesis using native chemical ligation
title_sort optimisation of chemical protein cleavage for erythropoietin semi-synthesis using native chemical ligation
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2898651/
https://www.ncbi.nlm.nih.gov/pubmed/18931805
http://dx.doi.org/10.1039/b811501j
work_keys_str_mv AT richardsonjonathanp optimisationofchemicalproteincleavageforerythropoietinsemisynthesisusingnativechemicalligation
AT macmillanderek optimisationofchemicalproteincleavageforerythropoietinsemisynthesisusingnativechemicalligation

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