ArticleChemical science2024
Fluorescent carbazole-derived α-amino acids: structural mimics of tryptophan.
Article in Chemical science, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 7 citations in OpenAlex.
- A general strategy towards multicolour fluorogenic peptides for wash-free bioassays.Nature chemistry · 2026Article
- Design, Synthesis, and Applications of Fluorescent Amino Acids in Bioimaging.Chemical & biomedical imaging · 2026Review
- A novel cyan-emitting fluorescent α-amino acid: synthesis, photophysical characterization and live-cell imaging properties.RSC advances · 2026Article
- Expanding the fluorescence toolkit: molecular design, synthesis and biological application of unnatural amino acids.Chemical science · 2025Review
- Synthesis of Fluorescent Dibenzofuran α-Amino Acids: Conformationally Rigid Analogues of Tyrosine.Organic letters · 2025Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Fluorescent tags are commonly used for imaging of proteins and peptides during biological events; however, the large size of dyes can disrupt protein structure and function, and typically require the use of a chemical spacer. Herein, we report the synthesis of a new class of fluorescent unnatural α-amino acid, containing carbazole side-chains designed to mimic l-tryptophan and thus, readily incorporated into peptides. The amino acids were constructed using a Negishi cross-coupling reaction as the key step and exhibited strong fluorescent emission, with high quantum yields in both organic solvents and water. Compatible with solid phase peptide synthesis, the carbazole amino acids were used to replace tryptophan in a β-hairpin model peptide and shown to be a close structural mimic with retention of conformation. They were also found to be effective fluorescent molecular reporters for biological events. Incorporation into a proline-rich ligand of the WW domain protein demonstrated that the fluorescent properties of a carbazole amino acid could be used to measure the protein-protein binding interaction of this important biological signalling process.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.