Department of Chemistry, Boston College, 2609 Beacon Street, 246B Merkert Chemistry Center, Chestnut Hill, MA, 02467, USA.
Chembiochem. 2018 Jul 4;19(13):1375-1378. doi: 10.1002/cbic.201800111. Epub 2018 Jun 1.
Approaches that enable the chemoselective, covalent modification of proteins in a site-specific manner have emerged as a powerful technology for a wide range of applications. The electron-rich unnatural amino acid 5-hydroxytryptophan was recently genetically encoded in both Escherichia coli and eukaryotes, thereby allowing its site-specific incorporation into virtually any recombinant protein. Herein, we report the chemoselective conjugation of various aromatic amines to full-length proteins under mild, oxidative conditions that target this site-specifically incorporated 5-hydroxytryptophan residue.
近年来，出现了一些可实现蛋白质化学选择性、共价修饰的方法，这些方法已成为广泛应用的强大技术。富电子非天然氨基酸 5-羟色氨酸最近在大肠杆菌和真核生物中被基因编码，从而可实现其在几乎任何重组蛋白中的定点掺入。在此，我们报告了在温和的氧化条件下，各种芳胺与全长蛋白质的化学选择性偶联，该反应靶向定点掺入的 5-羟色氨酸残基。
