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Enzymatic Modification of N-Terminal Proline Residues Using Phenol Derivatives

preprint
submitted on 29.09.2018 and posted on 01.10.2018 by Johnathan Maza, Daniel Bader, Lifeng Xiao, Alan Marmelstein, Daniel D. Brauer, Adel M. ElSohly, Matthew J. Smith, Matthew Francis
A convenient enzymatic strategyis reported for the modification of proline residues in the N-terminal positions of proteins. Using a tyrosinase enzyme isolated from Agaricus bisporus(abTYR), phenols and catechols are oxidized to highly reactive o-quinone intermediates that then couple to N-terminal proline residues in high yield. Key advantages of this bioconjugation method include (1) the use of air-stable precursors that can be prepared on large scale if needed, (2) mild reaction conditions, including low temperatures, (3) the targeting of native functional groups that can be introduced readily on most proteins, and (4) the use of molecular oxygen as the sole oxidant. This coupling strategy was successfully demonstrated for the attachment of a variety of phenol-derivatized cargo molecules to a series of protein substrates, including self-assembled viral capsids, enzymes, and a chitin binding domain (CBD). The ability of the CBD to bind to the surfaces of yeast cells was found to be unperturbed by this modification reaction.

History

Email Address of Submitting Author

jcmaza@berkeley.edu

Institution

University of California at Berkeley

Country

United States of America

ORCID For Submitting Author

0000-0003-2898-8770

Declaration of Conflict of Interest

No conflict of interest

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in Journal of the American Chemical Society

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