Journal
ORGANIC & BIOMOLECULAR CHEMISTRY
Volume 14, Issue 18, Pages 4194-4198Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c6ob00450d
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Funding
- National Basic Research Program of China (973 program) [2013CB932800]
- NSFC [21532004, 21225207, 21402206]
- Natural Science Foundation of Anhui Province [1508085QB30]
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A new thiol protecting group Hmb(off/on) is described, which has a switchable activity that may be useful in the chemical synthesis of proteins. When placed on the side chain of Cys, Cys(Hmb(off)) is stable to trifluoroacetic acid (TFA) in the process of solid-phase peptide synthesis. When Cys(Hmb(off)) is treated with neutral aqueous buffers, it is cleanly converted to acid-labile Cys(Hmb(on)), which can later be fully deprotected by TFA to generate free Cys. The utility of Cys(Hmb(off/on)) is demonstrated by the chemical synthesis of an erythropoietin segment, EPO[Cys(98)-Arg(166)]-OH through native chemical ligation.
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