Tyrosine-Specific Chemical Modification with in Situ Hemin-Activated Luminol Derivatives
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- 作者：Shinichi Sato ; Kosuke Nakamura ; Hiroyuki Nakamura
- 刊名：ACS Chemical Biology
- 出版年：2015
- 出版时间：November 20, 2015
- 年：2015
- 卷：10
- 期：11
- 页码：2633-2640
- 全文大小：412K
- ISSN：1554-8937
文摘
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鈥揳lkyne 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.