Angle-Resolved Linear Dichroism to Probe the Organization of Highly Ordered Collagen Biomaterials

• Published in: Biomacromolecules 2024-09, Vol.25 (9), p.6181-6187
• Main Authors: Krins, Natacha, Wien, Frank, Schmeltz, Margaux, Pérez, Javier, Dems, Dounia, Debons, Nicolas, Laberty-Robert, Christel, Schanne-Klein, Marie-Claire, Aimé, Carole
• Format: Article
• Language: English
• Subjects: Animals; Biocompatible Materials - chemistry; Chemical Sciences; Circular Dichroism - methods; Collagen - chemistry; X-Ray Diffraction - methods
• ISSN: 1525-7797; 1526-4602; 1526-4602
• DOI: 10.1021/acs.biomac.4c00860

Controlling the assembly of high-order structures is central to soft-matter and biomaterial engineering. Angle-resolved linear dichroism can probe the ordering of chiral collagen molecules in the dense state. Collagen triple helices were aligned by solvent evaporation. Their ordering gives a strong linear dichroism (LD) that changes sign and intensity with varying sample orientations with respect to the beam linear polarization. Being complementary to circular dichroism, which probes the structure of chiral (bio)­molecules, LD can shift from the molecular to the supramolecular scale and from the investigation of the conformation to interactions. Supported by multiphoton microscopy and X-ray scattering, we show that LD provides a straightforward route to probe collagen alignment, determine the packing density, and monitor denaturation. This approach could be adapted to any assembly of chiral (bio)­macromolecules, with key advantages in detecting large-scale assemblies with high specificity to aligned and chiral molecules and improved sensitivity compared to conventional techniques.