ArticleMolecules (Basel, Switzerland)2026
Interaction of Lysozyme with Sulfated β-Cyclodextrin: Dissecting Salt and Hydration Contributions.
Article in Molecules (Basel, Switzerland), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
2 citing papers in PubMed.
- Affibody Complex Formation: An In-Depth Thermodynamic Analysis Using Isothermal Titration Calorimetry.Molecules (Basel, Switzerland) · 2026Article
- Environmental Impact of β-Cyclodextrin Complexes with Herbicides: A Study on Solubility and Toxicity.Molecules (Basel, Switzerland) · 2026Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author.
Funding
Abstract
This article investigates the thermodynamic driving force of the interaction between lysozyme (Lys) and sulfated β-cyclodextrin (β-CDS), with a particular emphasis on the elusive role of hydration during polyelectrolyte-protein binding. Using isothermal titration calorimetry (ITC), the binding affinity was quantified across varying temperatures and salt concentrations, employing a recently developed thermodynamic framework that explicitly separates the contributions from counterion release and hydration effects. The study reveals that while counterion release is minimal in the Lys/β-CDS system, hydration effects become a dominant factor influencing the binding free energy Δ
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Registered trials
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