ArticleJournal of the Royal Society, Interface2022
Molecular rotors in haemoglobin and bovine serum albumin proteins.
Article in Journal of the Royal Society, Interface, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed, 5 citations in OpenAlex.
- Viscosity and density measurements on the cytosol of human red blood cells.Biophysical journal · 2025Article
- Molecular Rotors: Fluorescent Sensors for Microviscosity and Conformation of Biomolecules.Angewandte Chemie (International ed. in English) · 2024Review
Corrections and comments
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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
Molecular rotors are fluorescent viscosity probes and their response in simple fluids is known to be a Förster-Hoffman power law, allowing the viscosity of the medium to be quantified by its fluorescence intensity. They are attractive probes in biological media, usually consisting of proteins, but how does a molecular rotor behave in a protein solution? The response of the DASPI molecular rotor is compared in two globular protein solutions of similar size, haemoglobin (Hb) and bovine serum albumin, one absorbent, the other not. In absorbent Hb, a model validated by experiments in triangular geometry allows one to correct the absorbing effect and to compare the rotor response in both proteins. With concomitant microrheology measurements, we investigate the relation between the DASPI fluorescence intensity and solution viscosity. In protein solutions, we show that viscosity is no longer the parameter determining the rotor response in contrast to simple fluids. Varying the viscosity by concentration or temperature is not equivalent, and the Förster-Hoffmann power laws do not apply when the solution concentration varies. We show that the concentration regime of the protein solution, semi-dilute or concentrated, determines the sensitivity of the rotor to its environment.
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