Utilization of alkyne bioconjugations to modulate protein function

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• 作者：Johnathan C. Maza¹ ; Christina A. Howard¹ ; Megha A. Vipani ; Christopher R. Travis ; Douglas D. Young ; ^{dyoung01@wm.edu}
• 关键词：Bioconjugations ; Green fluorescent protein ; Glaser-Hay reaction ; Unnatural amino acids
• 刊名：Bioorganic & Medicinal Chemistry Letters
• 出版年：2017
• 出版时间：1 January 2017
• 年：2017
• 卷：27
• 期：1
• 页码：30-33
• 全文大小：620 K
• 卷排序：27

文摘

The ability to introduce or modify protein function has widespread application to multiple scientific disciplines. The introduction of unique unnatural amino acids represents an excellent mechanism to incorporate new functionality; however, this approach is limited by ability of the translational machinery to recognize and incorporate the chemical moiety. To overcome this potential limitation, we aimed to exploit the functionality of existing unnatural amino acids to perform bioorthogonal reactions to introduce the desired protein modification, altering its function. Specifically, via the introduction of a terminal alkyne containing unnatural amino acid, we demonstrated chemically programmable protein modification through the Glaser-Hay coupling to other terminal alkynes, altering the function of a protein. In a proof-of-concept experiment, this approach has been utilized to modify the fluorescence spectrum of green fluorescent protein.