Shinichi Sato, Kosuke Nakamura, and Hiroyuki Nakamura*
Chemical Resources Laboratory, Tokyo Institute
of Technology, Yokohama 226-8503, Japan
ACS Chem. Biol., Article ASAP
DOI: 10.1021/acschembio.5b00440
Publication Date (Web): September 10, 2015
Copyright © 2015 American Chemical Society
*E-mail: hiro@res.titech.ac.jp.
http://pubs.acs.org/doi/10.1021/acschembio.5b00440
Abstract
Tyrosine-specific chemical modification was achieved using in situ
hemin-activated luminol derivatives. Tyrosine residues in peptide and
protein were modified effectively with N-methylated luminol derivatives
under oxidative conditions in the presence of hemin and H2O2.
Both single and double modifications of the tyrosine residue occurred
in the reaction of angiotensin II with N-methylated luminol derivative 9.
Tyrosine-specific chemical modification of the model protein bovine
serum albumin (BSA) revealed that the surface-exposed tyrosine residues
were selectively modified with 9. We succeeded in the functionalization of several proteins using azide-conjugated compound 18
using alkyne-conjugated probes by copper(I)-catalyzed azide–alkyne
cycloaddition (CuAAC) or dibenzocyclooctyne (DBCO)-mediated copper-free
click chemistry. This tyrosine-specific modification was orthogonal to
conventional lysine modification by N-hydroxysuccinimide (NHS)
ester, and dual functionalization by fluorescence modification of
tyrosine residues and PEG modification of lysine residues was achieved
without affecting the modification efficiency.
コメント