@article{d108a65b10724d93a1923574eebe92db,
title = "Improving the fluorescent probe acridonylalanine through a combination of theory and experiment",
abstract = "Acridonylalanine (Acd) is a useful fluorophore for studying proteins by fluorescence spectroscopy, but it can potentially be improved by being made longer wavelength or brighter. Here, we report the synthesis of Acd core derivatives and their photophysical characterization. We also performed ab initio calculations of the absorption and emission spectra of Acd derivatives, which agree well with experimental measurements. The amino acid aminoacridonylalanine (Aad) was synthesized in forms appropriate for genetic incorporation and peptide synthesis. We show that Aad is a superior F{\"o}rster resonance energy transfer acceptor to Acd in a peptide cleavage assay and that Aad can be activated by an aminoacyl tRNA synthetase for genetic incorporation. Together, these results show that we can use computation to design enhanced Acd derivatives, which can be used in peptides and proteins.",
keywords = "Acridone, amino acid, electronic structure calculation, fluorescence spectroscopy",
author = "Itthipol Sungwienwong and Ferrie, \{John J.\} and Jun, \{Joomyung V.\} and Chunxiao Liu and Barrett, \{Taylor M.\} and Hostetler, \{Zachary M.\} and Naoya Ieda and Amara Hendricks and Muthusamy, \{Anand K.\} and Kohli, \{Rahul M.\} and Chenoweth, \{David M.\} and Petersson, \{George A.\} and Petersson, \{E. James\}",
note = "This work was supported by the University of Pennsylvania and the by the National Science Foundation (NSF; CHE-1708759 to EJP). Instruments supported by the National Institutes of Health (NIH) and NSF include MALDI MS (NSF, MRI-0820996); LCMS and HRMS (NIH, RR-023444); stopped flow fluorometer (NSF, CHE-1337449); and NMR (NIH, RR-022442). We thank the following for fellowship support: Royal Thai Foundation (IS), NSF Graduate Research Fellowship Program (DGE-1321851, JJF), NIH Chemistry Biology Interface Training Program (T32 GM071399, TMB and ZMH), and the Japan Society for the Promotion of Science (NI). The computational component of this research was supported by Temple University, Gaussian, Inc., and by the NSF (MRI-1625061) This work was supported by the University of Pennsylvania and the by the National Science Foundation (NSF; CHE‐1708759 to EJP). Instruments supported by the National Institutes of Health (NIH) and NSF include MALDI MS (NSF, MRI‐0820996); LCMS and HRMS (NIH, RR‐023444); stopped flow fluorometer (NSF, CHE‐1337449); and NMR (NIH, RR‐022442). We thank the following for fellowship support: Royal Thai Foundation (IS), NSF Graduate Research Fellowship Program (DGE‐1321851, JJF), NIH Chemistry Biology Interface Training Program (T32 GM071399, TMB and ZMH), and the Japan Society for the Promotion of Science (NI). The computational component of this research was supported by Temple University, Gaussian, Inc., and by the NSF (MRI‐ 1625061) Funding information: University of Pennsylvania; National Institutes of Health (NIH), Grant/Award Numbers: RR‐023444, RR‐022442 and GM‐071399; National Science Foundation (NSF), Grant/Award Numbers: CHE‐1708759, MRI‐0820996, CHE‐1337449, MRI‐1625061 and DGE‐1321851; Royal Thai Foundation; Japan Society for the Promotion of Science; Temple University; Gaussian Inc. Itthipol Sungwienwong and John J. Ferrie contributed equally to this work. This article is published in Journal of Physical Organic Chemistry as a special issue to celebrate the 100th birthday of Professor Jack Roberts.",
year = "2018",
month = aug,
doi = "10.1002/poc.3813",
language = "English (US)",
volume = "31",
journal = "Journal of Physical Organic Chemistry",
issn = "0894-3230",
publisher = "John Wiley \& Sons, Ltd.",
number = "8",
}