TY - JOUR
T1 - Tyrosine-Specific Chemical Modification with in Situ Hemin-Activated Luminol Derivatives
AU - Sato, Shinichi
AU - Nakamura, Kosuke
AU - Nakamura, Hiroyuki
N1 - Publisher Copyright:
© 2015 American Chemical Society.
PY - 2015/11/20
Y1 - 2015/11/20
N2 - 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.
AB - 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.
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U2 - 10.1021/acschembio.5b00440
DO - 10.1021/acschembio.5b00440
M3 - Article
C2 - 26356088
AN - SCOPUS:84947918378
VL - 10
SP - 2633
EP - 2640
JO - ACS Chemical Biology
JF - ACS Chemical Biology
SN - 1554-8929
IS - 11
ER -