Selective N-terminal acylation of peptides and proteins with a Gly-His tag sequence.

ABSTRACT: Methods for site-selective chemistry on proteins are in high demand for the synthesis of chemically modified biopharmaceuticals, as well as for applications in chemical biology, biosensors and more. Inadvertent N-terminal gluconoylation has been reported during expression of proteins with an N-terminal His tag. Here we report the development of this side-reaction into a general method for highly selective N-terminal acylation of proteins to introduce functional groups. We identify an optimized N-terminal sequence, GHHH_n- for the reaction with gluconolactone and 4-methoxyphenyl esters as acylating agents, facilitating the introduction of functionalities in a highly selective and efficient manner. Azides, biotin or a fluorophore are introduced at the N-termini of four unrelated pr

SUBMITTER: Martos-Maldonado MC 

PROVIDER: S-EPMC6098153 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature