ArticleJournal of fluorescence2010
Effect of 1-aminoanthracene (1-AMA) binding on the structure of three lipocalin proteins, the dimeric β lactoglobulin, the dimeric odorant binding protein and the monomeric α1-acid glycoprotein. Fluorescence spectra and lifetimes studies.
Article in Journal of fluorescence, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 19 citations in OpenAlex.
- Biophysical insights into a cryptic ligand site in the hydrophobic core of human PCNA.Biophysical journal · 2026Article
- Photophysical Investigation of Dyes and Dye-PMMA Systems: Insights into Absorption, Emission, and Charge Transfer Mechanisms.The journal of physical chemistry. A · 2025Article
- Two Engineered OBPs with opposite temperature-dependent affinities towards 1-aminoanthracene.Scientific reports · 2018Article
- Article
- Energy transfer studies between Trp residues of three lipocalin proteins family, α1-acid glycoprotein, (orosomucoid), β-lactoglobulin and porcine odorant binding protein and the fluorescent probe, 1-aminoanthracene (1-AMA).Journal of fluorescence · 2015Article
- Origin of tryptophan fluorescence lifetimes part 1. Fluorescence lifetimes origin of tryptophan free in solution.Journal of fluorescence · 2014Article
- Origin of tryptophan fluorescence lifetimes. Part 2: fluorescence lifetimes origin of tryptophan in proteins.Journal of fluorescence · 2014Article
- Relation between proteins tertiary structure, tryptophan fluorescence lifetimes and tryptophan S(o)→(1)L(b) and S(o)→(1)L(a) transitions. Studies on α1-acid glycoprotein and β-lactoglobulin.Journal of fluorescence · 2011Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
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Abstract
We studied effect of 1-aminoanthracene (1-AMA) binding on the structures of dimeric β lactoglobulin, dimeric odorant binding protein (OBP) and monomeric α(1)-acid glycoprotein (lipocalin family proteins) by monitoring fluorescence excitation spectra and measuring fluorescence lifetimes of the tryptophan residues of the proteins. Results show that binding of 1-AMA to β lactoglobulin and OBP modifies their conformation even at low probe concentration compared to that of the proteins. Structural modification induces a red shift of the fluorescence excitation spectra maximum of tryptophan residues accompanied with an increase of the third fluorescence lifetime and a decrease of its pre-exponential factor. These effects were not observed for α(1)-acid glycoprotein, probably as the result of carbohydrate presence. These data raise doubts concerning use of 1-AMA as a probe to study biological properties of β lactoglobulin and OBP.
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