用于蛋白质化学修饰的呋喃基乙酰化剂。

Furan-based acetylating agent for the chemical modification of proteins.

作者信息

De Sudipta, Kumar Tarun, Bohre Ashish, Singh Laishram R, Saha Basudeb

机构信息

Laboratory of Catalysis, Department of Chemistry, University of Delhi, North Campus, Delhi 110007, India.

Dr. B.R. Ambedkar Centre for Biomedical Research, University of Delhi, North Campus, Delhi 110007, India.

出版信息

Bioorg Med Chem. 2015 Feb 15;23(4):791-6. doi: 10.1016/j.bmc.2014.12.053. Epub 2014 Dec 30.

DOI:10.1016/j.bmc.2014.12.053

PMID:25596165

Abstract

We have synthesized a furan-based acetylating agent, 2,5-bisacetoxymethylfuran (BAMF) from carbohydrate derived 5-hydroxymethylfurfural (HMF) and studied its acetylation activity with amines and cytochrome c. The results show that BAMF can modify proteins in biological conditions without affecting their structure and function. The modification of cytochrome c with BAMF occurred through the reduction of heme center, but there was no change in the coordination property of iron and the tertiary structure of cytochrome c. Further analysis using MALDI-TOF-MS spectrometer suggests that BAMF selectively targeted lysine amino acid of cytochrome c under our experimental conditions. Kinetics study revealed that the modification of cytochrome c with BAMF took place at faster rates than aspirin.

摘要

我们从碳水化合物衍生的5-羟甲基糠醛（HMF）合成了一种基于呋喃的乙酰化剂2,5-双乙酰氧基甲基呋喃（BAMF），并研究了其与胺类和细胞色素c的乙酰化活性。结果表明，BAMF可在生物条件下修饰蛋白质而不影响其结构和功能。BAMF对细胞色素c的修饰是通过血红素中心的还原发生的，但铁的配位性质和细胞色素c的三级结构没有变化。使用基质辅助激光解吸电离飞行时间质谱仪（MALDI-TOF-MS）的进一步分析表明，在我们的实验条件下，BAMF选择性地靶向细胞色素c的赖氨酸氨基酸。动力学研究表明，BAMF对细胞色素c的修饰速率比阿司匹林更快。