ArticleJournal of fluorescence2017
Sensing Tryptophan Microenvironment of Amyloid Protein Utilizing Wavelength-Selective Fluorescence Approach.
Article in Journal of fluorescence, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 18 citations in OpenAlex.
- Recent Developments of Hybrid Fluorescence Techniques: Advances in Amyloid Detection Methods.Current protein & peptide science · 2024Review
- Red edge excitation shift spectroscopy is highly sensitive to tryptophan composition.Journal of the Royal Society, Interface · 2023Article
- Chemical Mapping Exposes the Importance of Active Site Interactions in Governing the Temperature Dependence of Enzyme Turnover.ACS catalysis · 2021Article
- Fluorescence-based techniques for the detection of the oligomeric status of proteins: implication in amyloidogenic diseases.European biophysics journal : EBJ · 2021Review
- Novel insights in linking solvent relaxation dynamics and protein conformations utilizing red edge excitation shift approach.Emerging topics in life sciences · 2021Review
- Monoclonal antibody stability can be usefully monitored using the excitation-energy-dependent fluorescence edge-shift.The Biochemical journal · 2020Article
- Wavelength-Selective Fluorescence of a Model Transmembrane Peptide: Constrained Dynamics of Interfacial Tryptophan Anchors.Journal of fluorescence · 2018Article
- Aggregation Behavior of pHLIP in Aqueous Solution at Low Concentrations: A Fluorescence Study.Journal of fluorescence · 2018Article
- GFP fluorescence: A few lesser-known nuggets that make it work.Journal of biosciences · 2018Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Structural transition among various forms of proteins involves subtle interplay between structure and dynamics and is crucial in human diseases. Red edge excitation shift (REES) represents a suitable approach to explore the environmental organization and dynamics surrounding tryptophan residues in proteins. Although REES from tryptophan residues has been reported for native, molten globule and denatured states of proteins, such data on the amyloid form of proteins is lacking. κ-casein is one of the most important constituents of casein micelles in milk and has a tendency to form amyloid fibril. We report here REES of the sole tryptophan residue for native, acid-denatured and urea-denatured forms of κ-casein. More importantly, we show that the amyloid form of κ-casein displays REES of 4 nm. We analyze these results in terms of tryptophan microenvironment in various forms of κ-casein, particularly the amyloid form. We conclude that REES is a sensitive tool to monitor structural plasticity in proteins.
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