Journal
ACS CHEMICAL BIOLOGY
Volume 10, Issue 11, Pages 2633-2640Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acschembio.5b00440
Keywords
-
Categories
Funding
- MEXT, Japan [26102721, 25810104, 15H01372]
- Grants-in-Aid for Scientific Research [15H01372, 15H05490, 25810104, 26102721, 15K12742] Funding Source: KAKEN
Ask authors/readers for more resources
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 H(2)O2. 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 azidealkyne 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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available