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In the quest to identify a property that may reliably predict the spontaneity of a process, a promising candidate has been identified: entropy. Processes that involve an increase in entropy of the system (ΔS > 0) are very often spontaneous; however, examples to the contrary are plentiful. By expanding consideration of entropy changes to include the surroundings, a significant conclusion regarding the relation between this property and spontaneity may be reached. In thermodynamic models, the...

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Related Experiment Video

Updated: Feb 10, 2026

Measuring Biomolecular DSC Profiles with Thermolabile Ligands to Rapidly Characterize Folding and Binding Interactions

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[Thermodynamic parameters characterizing interaction between ligand molecules adsorbed on a polymer]

Iu D Nechipurenko

|May 1, 1982

Summary

This study introduces a new method to analyze ligand-polymer interactions by modeling potentials. The approach quantifies interaction energy and distance, applicable to drug-DNA binding analysis.

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Area of Science:

Polymer science
Biophysics
Computational chemistry

Context:

Understanding ligand-polymer interactions is crucial for drug delivery and biomaterials.
Existing models often simplify the complex interplay between adsorbed molecules.
The adsorption of ligands onto polymer surfaces is a fundamental process in various scientific fields.

Purpose:

To develop a novel method for characterizing paired interactions between adsorbed ligand molecules on polymers.
To describe these interactions using simplified potential shapes (rectangular and trapezoidal).
To enable the analysis of experimental adsorption isotherms for quantitative insights.

Summary:

A procedure was developed to recognize potentials of paired interactions between ligand molecules adsorbed on a polymer.
A method using rectangular and trapezoidal potentials is proposed to describe these interactions.
When interactions extend beyond mean distances, adsorption follows non-cooperative binding expressions, allowing for method development.

Impact:

The developed method allows for the estimation of interaction energy and effective distance between adsorbed ligands.
This technique provides a way to analyze experimental adsorption isotherms, offering deeper understanding of molecular interactions.
The method was successfully applied to analyze the adsorption of distamycin A antibiotic on poly(dG) . poly(dC) DNA, demonstrating its practical utility in biophysical studies.