蛋白质翻译后修饰是蛋白质功能多样化扩展的重要方式，多数是在酶催化下完成的化学反应。蛋白交联、修饰和标记则是科学家学习和模拟这些蛋白质天然化学转化，并用于研究蛋白结构和相互作用的常用技术。本项目拟借助我们在天然产物chlorofusin合成中发现的azaphilone和伯胺之间的温和高效交联反应，将结构独特的azaphilone化合物经过一定的修饰和结构变化，发展为温和、无痕迹、高效率的天然蛋白赖氨酸氨基的交联标记物和分子工具；以azaphilone为分子支架，设计、合成和发展若干蛋白质标记方法和蛋白质固载化方法。

Protein post-translational modification is the most important native chemical reactions aided by enzyme(s) under biological conditions. To learn and mimic the native biological transformations, chemical modification of proteins has now been becoming an important tool for probing natural systems and protein-protein interactions, creating therapeutic conjugates, and generating novel protein constructs as well. Based on our previous discovery of a mild efficient conjugation reaction between the unique azaphilone and various primary amines, including amino acids and amino-cyclopeptides, during our long-term study on the total synthesis of natural product chlorofusin, we wish to further develop azaphilones to be a new type of efficient traceless bioconjugation reagents for labeling the lysine(s) of native proteins after necessary structural modifications under this project. Also, it is planned to explore the potential of applying azaphilone-headed molecular tools for protein multi-labeling and protein immobilization after proper molecular design, organic synthesis and condition optimization.