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Chemoselective Dual Labeling of Native and Recombinant Proteins.

ABSTRACT: The attachment of two different functionalities in a site-selective fashion represents a great challenge in protein chemistry. We report site specific dual functionalizations of peptides and proteins capitalizing on reactivity differences of cysteines in their free (thiol) and protected, oxidized (disulfide) forms. The dual functionalization of interleukin 2 and EYFP proceeded with no loss of bioactivity in a stepwise fashion applying maleimide and disulfide rebridging allyl-sulfone groups. In order to ensure broader applicability of the functionalization strategy, a novel, short peptide sequence that introduces a disulfide bridge was designed and site-selective dual labeling in the presence of biogenic groups was successfully demonstrated.

SUBMITTER: Agrawalla BK

PROVIDER: S-EPMC6242188 | biostudies-literature | 2018 Jan

REPOSITORIES: biostudies-literature

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Chemoselective Dual Labeling of Native and Recombinant Proteins.

Agrawalla Bikram Keshari BK Wang Tao T Riegger Andreas A Domogalla Matthias P MP Steinbrink Kerstin K Dörfler Thilo T Chen Xi X Boldt Felix F Lamla Markus M Michaelis Jens J Kuan Seah Ling SL Weil Tanja T

Bioconjugate chemistry 20171220 1

The attachment of two different functionalities in a site-selective fashion represents a great challenge in protein chemistry. We report site specific dual functionalizations of peptides and proteins capitalizing on reactivity differences of cysteines in their free (thiol) and protected, oxidized (disulfide) forms. The dual functionalization of interleukin 2 and EYFP proceeded with no loss of bioactivity in a stepwise fashion applying maleimide and disulfide rebridging allyl-sulfone groups. In o ...[more]

PMID: 29231709

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