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Interaction of anionic compounds with gelatin. I: Binding studies

J Gautam¹, H Schott

¹School of Pharmacy, Temple University, Philadelphia, PA 19140.

Journal of Pharmaceutical Sciences

|July 1, 1994

Summary

This study investigated how gelatin interacts with small organic molecules like azo dyes, which model anionic drugs. Gelatin

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Area of Science:

Pharmaceutical Science
Polymer Chemistry
Physical Chemistry

Background:

Gelatin is a widely used pharmaceutical excipient.
Interactions between gelatin and small organic molecules, particularly anionic drugs, are not well understood.
Azo dyes serve as effective models for anionic drugs due to their structural similarities.

Purpose of the Study:

To investigate the binding interactions between gelatin and four different azo dyes.
To understand how factors like pH, temperature, and solvent composition affect dye-gelatin binding.
To characterize the thermodynamic parameters of the binding process.

Main Methods:

Ultrafiltration was used to separate bound and free dye.
Spectrophotometric assays quantified dye concentrations.
pH shift measurements provided an alternative binding assessment.
Binding isotherms were analyzed to determine binding limits and characteristics.

Main Results:

Binding isotherms showed two linear segments, indicating partitioning and a binding limit.
pH influenced binding differently for sulfonated and carboxylated dyes, with similar binding at pH >= 7.00.
Binding decreased with increasing temperature, indicating exothermic binding (negative enthalpy).
Changes in solvent and decreased hydrocarbon moiety size also reduced binding.

Conclusions:

Gelatin exhibits reversible binding with azo dyes, characterized by negative entropy changes.
The study provides insights into gelatin-dye interactions, relevant for anionic drug formulation.
Understanding these interactions is crucial for optimizing drug delivery and stability in pharmaceutical products.

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