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Molecules 2017, 22(7), 1194; doi:10.3390/molecules22071194

Fluorescence Modulation of Green Fluorescent Protein Using Fluorinated Unnatural Amino Acids

Department of Chemistry, The College of William & Mary, Williamsburg, VA 231871, USA
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Authors to whom correspondence should be addressed.
Received: 26 June 2017 / Revised: 12 July 2017 / Accepted: 13 July 2017 / Published: 16 July 2017
(This article belongs to the Section Bioorganic Chemistry)
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Abstract

The ability to modulate protein function through minimal perturbations to amino acid structure represents an ideal mechanism to engineer optimized proteins. Due to the novel spectroscopic properties of green fluorescent protein, it has found widespread application as a reporter protein throughout the fields of biology and chemistry. Using site-specific amino acid mutagenesis, we have incorporated various fluorotyrosine residues directly into the fluorophore of the protein, altering the fluorescence and shifting the pKa of the phenolic proton associated with the fluorophore. Relative to wild type GFP, the fluorescence spectrum of the protein is altered with each additional fluorine atom, and the mutant GFPs have the potential to be employed as pH sensors due to the altered electronic properties of the fluorine atoms. View Full-Text
Keywords: unnatural amino acids; green fluorescent protein; biosensors; fluorotyrosine unnatural amino acids; green fluorescent protein; biosensors; fluorotyrosine
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Villa, J.K.; Tran, H.-A.; Vipani, M.; Gianturco, S.; Bhasin, K.; Russell, B.L.; Harbron, E.J.; Young, D.D. Fluorescence Modulation of Green Fluorescent Protein Using Fluorinated Unnatural Amino Acids. Molecules 2017, 22, 1194.

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