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- W4200317227 abstract "The site-specific incorporation of nonstandard amino acids (nsAAs) during translation has expanded the chemistry and function of proteins. The nsAA para-azido-phenylalanine (pAzF) encodes a biorthogonal chemical moiety that facilitates click reactions to attach diverse chemical groups for protein functionalization. However, the azide moiety is unstable in physiological conditions and is reduced to para-amino-phenylalanine (pAF). Azide reduction decreases the yield of pAzF residues in proteins to 50%-60% per azide and limits protein functionalization by click reactions. Here, we describe the use of a pH-tunable diazotransfer reaction that converts pAF to pAzF at >95% efficiency in proteins. The method selectively restores pAzF at multiple sites per protein without introducing off-target modifications. This work addresses a key limitation in the production of pAzF-containing proteins by restoring azides for multi-site functionalization with diverse chemical moieties, setting the stage for the production of genetically encoded biomaterials with broad applications in biotherapeutics, materials science, and biotechnology." @default.
- W4200317227 created "2021-12-31" @default.
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- W4200317227 date "2022-06-01" @default.
- W4200317227 modified "2023-09-27" @default.
- W4200317227 title "Chemoselective restoration of para-azido-phenylalanine at multiple sites in proteins" @default.
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- W4200317227 doi "https://doi.org/10.1016/j.chembiol.2021.12.002" @default.
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