Document Type
Article
Department/Program
Chemistry
Journal Title
BIOORGANIC & MEDICINAL CHEMISTRY LETTERS
Pub Date
1-1-2017
Volume
27
Issue
1
Abstract
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. (C) 2016 Elsevier Ltd. All rights reserved.
Recommended Citation
Maza, Johnathan C.; Howard, Christina A.; Vipani, Megha A.; Travis, Christopher R.; and Young, Douglas D., Utilization of alkyne bioconjugations to modulate protein function (2017). BIOORGANIC & MEDICINAL CHEMISTRY LETTERS, 27(1).
https://doi.org/10.1016/j.bmcl.2016.11.041
DOI
https://doi.org/10.1016/j.bmcl.2016.11.041
