| Literature DB >> 30397320 |
Daniel T Cohen1,2, Chi Zhang3, Colin M Fadzen3, Alexander J Mijalis3, Liana Hie4, Kenneth D Johnson5, Zachary Shriver5, Obadiah Plante5, Scott J Miller4, Stephen L Buchwald3, Bradley L Pentelute6,7.
Abstract
Conjugates between proteins and small molecules enable access to a vast chemical space that is not achievable with either type of molecule alone; however, the paucity of specific reactions capable of functionalizing proteins and natural products presents a formidable challenge for preparing conjugates. Here we report a strategy for conjugating electron-rich (hetero)arenes to polypeptides and proteins. Our bioconjugation technique exploits the electrophilic reactivity of an oxidized selenocysteine residue in polypeptides and proteins, and the electron-rich character of certain small molecules to provide bioconjugates in excellent yields under mild conditions. This conjugation chemistry enabled the synthesis of peptide-vancomycin conjugates without the prefunctionalization of vancomycin. These conjugates have an enhanced in vitro potency for resistant Gram-positive and Gram-negative pathogens. Additionally, we show that a 6 kDa affibody protein and a 150 kDa immunoglobulin-G antibody could be modified without diminishing bioactivity.Entities:
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Year: 2018 PMID: 30397320 PMCID: PMC6454892 DOI: 10.1038/s41557-018-0154-0
Source DB: PubMed Journal: Nat Chem ISSN: 1755-4330 Impact factor: 24.427