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Related Experiment Video

Updated: May 10, 2026

Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides

Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides

Published on: January 31, 2014

Collagen functionalized with unsaturated cyclic anhydrides-interactions in solution and solid state.

S Potorac¹, M Popa, L Picton

¹Department of Natural and Synthetic Polymers, "Gheorghe Asachi", Technical University of Iasi, Faculty of Chemical Engineering and Environmental Protection, Str. D. Mangeron 73, 700050, Iasi, Romania; Normandie Université, France; Université de Rouen, Laboratoire Polymères Biopolymères Surfaces, F-76821, Mont Saint Aignan, France; CNRS UMR 6270 & FR3038, F-76821, Mont Saint Aignan, France.

|June 21, 2013

Summary

This summary is machine-generated.

Modified collagen with maleic anhydride (CMA) and itaconic anhydride (CITA) showed enhanced thermal stability and elastic properties. CITA exhibited a pronounced thixotropic behavior, indicating potential for advanced material applications.

Keywords:

collagen rheology temperature

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Production of Nanofibrillar Patterned Collagen for Tissue Engineering

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Published on: September 20, 2024

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Last Updated: May 10, 2026

Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides

Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides

Published on: January 31, 2014

Production of Nanofibrillar Patterned Collagen for Tissue Engineering

Production of Nanofibrillar Patterned Collagen for Tissue Engineering

Published on: September 20, 2024

Area of Science:

Biomaterials Science
Polymer Chemistry

Background:

Collagen is a key biomaterial with potential for various applications.
Modifying collagen can enhance its properties for specific uses, such as in interpenetrated polymer networks (IPN).

Purpose of the Study:

To prepare maleic anhydride (CMA) and itaconic anhydride (CITA) modified collagen as precursors for IPN production.
To investigate the solution behavior, rheological properties, and thermal stability of modified collagen.

Main Methods:

Synthesis of CMA and CITA modified collagen.
Rheological measurements (flow and oscillatory) to assess thixotropic and elastic behavior.
Differential Scanning Calorimetry (DSC) to determine denaturation temperature (Td).

Main Results:

Modified collagen solutions exhibited elastic behavior, with storage modulus (G') consistently higher than loss modulus (G″).
Itaconic anhydride-modified collagen (CITA) showed a pronounced thixotropic behavior in semi-diluted solutions.
Denaturation temperature increased significantly: from 34°C for unmodified collagen to 40°C for CMA-modified and 39°C for CITA-modified collagen, due to covalent bond formation stabilizing the triple helix.

Conclusions:

Covalent modification of collagen with maleic anhydride and itaconic anhydride enhances its thermal stability and alters its solution rheology.
The modified collagens are suitable precursors for interpenetrated polymer networks (IPN).
CITA-modified collagen's pronounced thixotropy suggests potential for shear-thinning applications.