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Multimodal AFM-IR nanospectroscopy and non-linear optical microscopy for detecting collagen matrix alterations.
Jérémie Mathurin1, Gaël Latour2,3, Gervaise Mosser4
1Institut de Chimie Physique, UMR 8000, Université Paris-Saclay, CNRS, 91405 Orsay, France. ariane.deniset@universite-paris-saclay.fr.
The Analyst
|March 9, 2026
Summary
Thermal esterification causes irreversible molecular changes in collagen, identified by a specific IR band. This finding reveals collagen
Area of Science:
- Biophysics
- Materials Science
- Biochemistry
Background:
- Collagen is a crucial structural protein.
- Understanding collagen's molecular alterations is vital for tissue engineering and disease research.
Purpose of the Study:
- To investigate the molecular origin of a specific infrared (IR) band in collagen.
- To identify markers of irreversible collagen structural changes.
Main Methods:
- Correlative Atomic Force Microscopy-Infrared Spectroscopy (AFM-IR).
- Nonlinear optical microscopy.
Main Results:
- A distinct 1730 cm⁻¹ IR band emerged in collagen.
- This band is attributed to local, thermally induced esterification.
- The band indicates irreversible molecular alteration and structural destabilization.
Conclusions:
- Thermally induced esterification is a key process leading to collagen degradation.
- The 1730 cm⁻¹ IR band serves as a reliable marker for irreversible collagen modification.
- These findings have implications for understanding aging and disease processes affecting collagen.
