Site-specific incorporation of a fluorescent terphenyl unnatural amino acid

被引：16

作者：

Lampkowski, Jessica S. ^{[1
]}

Uthappa, Diya M. ^{[1
]}

Young, Douglas D. ^{[1
]}

机构：

[1] Coll William & Mary, Dept Chem, Williamsburg, VA 23187 USA

来源：

BIOORGANIC & MEDICINAL CHEMISTRY LETTERS | 2015年 / 25卷 / 22期

关键词：

Unnatural amino acids; Green fluorescent protein; Fluorescent sensors; Protein expression; Aminoacyl-tRNA synthetase; EXPANDED GENETIC-CODE; ESCHERICHIA-COLI; LIVING CELLS; CHEMICAL AMINOACYLATION; FUSION PROTEINS; TRANSFER-RNA; P-TERPHENYL; PROBES; DYNAMICS; CONJUGATION;

D O I：

10.1016/j.bmcl.2015.09.050

中图分类号：

R914 [药物化学];

学科分类号：

100701 ;

摘要：

The site-specific incorporation of unnatural amino acids into proteins has a wide range of biological implications. Of particular interest is the incorporation of fluorescent probes as a mechanism to track protein function, transport, and folding. Thus, the development of a novel system for the incorporation of new fluorescent unnatural amino acids has significant utility. Specifically, we have elucidated an aminoacyl-tRNA synthetase capable of recognizing a terphenyl UAA derivative, and charging a cognate tRNA with this amino acid for protein incorporation. Moreover, we have successfully incorporated this fluorescent UAA into GFP at several key residues, demonstrating a novel means to modulate fluorescence within the protein. (C) 2015 Elsevier Ltd. All rights reserved.

引用

页码：5277 / 5280

页数：4

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