ArticleJournal of fluorescence2009
Fluorescence origin of 6,P-toluidinyl-naphthalene-2-sulfonate (TNS) bound to proteins.
Article in Journal of fluorescence, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 20 citations in OpenAlex.
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- Bacterial LPX motif-harboring virulence factors constitute a species-spanning family of cell-penetrating effectors.Cellular and molecular life sciences : CMLS · 2018Article
- T3SS-Independent Uptake of the Short-Trip Toxin-Related Recombinant NleC Effector of EnteropathogenicFrontiers in cellular and infection microbiology · 2017Article
- Origin of tryptophan fluorescence lifetimes part 1. Fluorescence lifetimes origin of tryptophan free in solution.Journal of fluorescence · 2014Article
- Sub-structures formed in the excited state are responsible for tryptophan residues fluorescence in β-lactoglobulin.Journal of fluorescence · 2011Article
- 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
- 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.Journal of fluorescence · 2010Article
- Glycosyl conjugates of biotinylated diaminopyridine applied for study of carbohydrate-to-carbohydrate interaction.Glycoconjugate journal · 2010Article
- Fluorescence lifetimes of tryptophan: structural origin and relation with So --> 1Lb and So --> 1La transitions.Journal of fluorescence · 2009Article
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Authors and funding
1 author.
Funding
No grant is acknowledged in the PubMed record.
Abstract
6,P-toluidinylnaphthalene-2-sulfonate (TNS) is a highly fluorescent molecule when dissolved in a low polarity medium or when bound to proteins. The aim of the present work is to explain origin of this fluorescence, to find out how the medium (solvent, protein matrix) affects fluorescence observables such as lifetimes and spectra and finally to put into evidence possible relation that exists between these observables and fluorophore structure. To achieve our goal we performed studies on TNS dissolved in ethanol, at high concentrations in water (aggregated form) and bound to proteins. Our experiments allowed us to find out that TNS in the three environments has different structures. Presence of three lifetimes observed in proteins and in water instead of one lifetime found in ethanol can be assigned to the high contact between TNS molecules. Our results are discussed in terms of solvent polarity and interaction within fluorophore molecules bound to proteins.
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