ArticleAnalytical biochemistry2015
Sensing pH via p-cyanophenylalanine fluorescence: Application to determine peptide pKa and membrane penetration kinetics.
Article in Analytical biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 14 citations in OpenAlex.
- Design, Synthesis, and Applications of Fluorescent Amino Acids in Bioimaging.Chemical & biomedical imaging · 2026Review
- Expanding the fluorescence toolkit: molecular design, synthesis and biological application of unnatural amino acids.Chemical science · 2025Review
- pH Effect on Two-Photon Cross Section of Highly Fluorescent Dyes Using Femtosecond Two-Photon Induced Fluorescence.Journal of fluorescence · 2017Article
- Minimalist IR and fluorescence probes of protein function.Current opinion in chemical biology · 2016Review
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
We expand the spectroscopic utility of a well-known infrared and fluorescence probe, p-cyanophenylalanine, by showing that it can also serve as a pH sensor. This new application is based on the notion that the fluorescence quantum yield of this unnatural amino acid, when placed at or near the N-terminal end of a polypeptide, depends on the protonation status of the N-terminal amino group of the peptide. Using this pH sensor, we are able to determine the N-terminal pKa values of nine tripeptides and also the membrane penetration kinetics of a cell-penetrating peptide. Taken together, these examples demonstrate the applicability of using this unnatural amino acid fluorophore to study pH-dependent biological processes or events that accompany a pH change.
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