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Factors Affecting Dissolution: Polymorphism, Amorphism and Pseudopolymorphism

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Polymorphism refers to the existence of a drug substance in multiple crystalline forms, known as polymorphs. Recently, this term has been expanded to include solvates (forms containing a solvent), amorphous forms (non-crystalline forms), and desolvated solvates (forms from which the solvent has been removed).
Some polymorphic crystals possess lower aqueous solubility than their amorphous counterparts, leading to incomplete absorption. For instance, the oral suspension of Chloramphenicol, which...

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Related Experiment Video

Updated: May 10, 2026

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy

Published on: June 27, 2014

Deciphering solid state photostability of polymyxin B using deconvolution based FTIR insights.

Aanchal Yadav¹, Pavankumar Sathala², Madhuri Divate²

¹Department of Biopharmaceuticals, National Institute of Pharmaceutical Education and Research- Guwahati (NIPER-G), Guwahati assam, India 781101.

Spectrochimica Acta. Part A, Molecular and Biomolecular Spectroscopy

|April 25, 2025

Summary

Polymyxin B antibiotic degrades rapidly when exposed to light, especially UV. Structural changes and degradation rates were analyzed under various light conditions and room temperature, revealing specific breakdown patterns in its peptide regions.

Keywords:

Cyclo-heptapeptide backbone Degradation Fatty acyl tail Photostability Polymyxin B Tripeptide deconvoluted FT-IR

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Last Updated: May 10, 2026

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy

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Area of Science:

Analytical Chemistry
Spectroscopy
Pharmaceutical Sciences

Background:

Polymyxin B is a crucial antibiotic with known instability issues.
Its solid-state photostability requires thorough investigation due to degradation susceptibility.
Understanding degradation pathways is vital for effective storage and formulation.

Purpose of the Study:

To investigate the solid-state photostability of Polymyxin B.
To elucidate structural changes under room temperature, UV, and visible light.
To determine degradation kinetics and identify vulnerable regions.

Main Methods:

Deconvolution-based Fourier Transform Infrared (FTIR) spectroscopy was employed.
Structural changes were analyzed across five defined spectral regions.
Photostability was assessed over 30 days under different light conditions.
Principal Component Analysis (PCA) was used to analyze degradation trends.

Main Results:

The cyclo-heptapeptide region showed the highest fragmentation rate, particularly under UV light.
Degradation followed second-order kinetics at room temperature and was higher under light exposure.
UV light primarily degraded peptide bonds, while visible light caused hydroxyl group oxidation.
The fatty acyl tail demonstrated greater stability against hydrolytic reactions.

Conclusions:

Polymyxin B exhibits differential degradation across its functional regions.
UV and visible light significantly accelerate degradation compared to room temperature.
Room temperature degradation follows zero-order kinetics in specific regions, enhanced by light exposure.
Insights into Polymyxin B's stability under various conditions are provided.