The effect of dehydrothermal treatment on the mechanical and structural properties of collagen‐GAG scaffolds
- 22 April 2008
- journal article
- research article
- Published by Wiley in Journal of Biomedical Materials Research Part A
- Vol. 89A (2), 363-369
- https://doi.org/10.1002/jbm.a.31955
Abstract
The mechanical properties of tissue engineering scaffolds are critical for preserving the structural integrity and functionality during both in vivo implantation and long-term performance. In addition, the mechanical and structural properties of the scaffold can direct cellular activity within a tissue-engineered construct. In this context, the aim of this study was to investigate the effects of dehydrothermal (DHT) treatment on the mechanical and structural properties of collagen-glycosaminoglycan (CG) scaffolds. Temperature (105–180°C) and exposure period (24–120 h) of DHT treatment were varied to determine their effect on the mechanical properties, crosslinking density, and denaturation of CG scaffolds. As expected, increasing the temperature and duration of DHT treatment resulted in an increase in the mechanical properties. Compressive properties increased up to twofold, while tensile properties increased up to 3.8-fold. Crosslink density was found to increase with DHT temperature but not exposure period. Denaturation also increased with DHT temperature and exposure period, ranging from 25% to 60% denaturation. Crosslink density was found to be correlated with compressive modulus, whilst denaturation was found to correlate with tensile modulus. Taken together, these results indicate that DHT treatment is a viable technique for altering the mechanical properties of CG scaffolds. The enhanced mechanical properties of DHT-treated CG scaffolds improve their suitability for use both in vitro and in vivo. In addition, this work facilitates the investigation of the effects of mechanical properties and denaturation on cell activity in a 3D environment. © 2008 Wiley Periodicals, Inc. J Biomed Mater Res, 2009Keywords
This publication has 43 references indexed in Scilit:
- Fourier transform infrared (FTIR) spectroscopic study of acid soluble collagen and gelatin from skins and bones of young and adult Nile perch (Lates niloticus)Food Chemistry, 2004
- Stabilization of low denaturation temperature collagen from fish by physical cross-linking methodsJournal of Bioscience and Bioengineering, 2003
- Tendon cell contraction of collagen–GAG matrices in vitro: effect of cross-linkingBiomaterials, 2000
- Collagen – biomaterial for drug deliveryEuropean Journal of Pharmaceutics and Biopharmaceutics, 1998
- Methods for the treatment of collagenous tissues for bioprosthesesBiomaterials, 1997
- The Kinetics of the Thermal Denaturation of Collagen in Unrestrained Rat Tail Tendon Determined by Differential Scanning CalorimetryJournal of Molecular Biology, 1995
- Successful Use of a Physiologically Acceptable Artificial Skin in the Treatment of Extensive Burn InjuryAnnals of Surgery, 1981
- Chemical cross-linking restrictions on models for the molecular organization of the collagen fibreNature, 1980
- Design of an artificial skin. Part III. Control of pore structureJournal of Biomedical Materials Research, 1980
- Cross-linking of Gelatine by DehydrationNature, 1967