Collagen gel is widely used in tissue engineering due to excellent biological properties and swollen three-dimensional network structure. To improve viscoelasticity and thermal stability, collagen gels consisting of fibrils were cross-linked with glutaraldehyde and sequentially dehydrated via ethanol or heating (named as EGC or HGC, respectively). For EGC, ethanol replaced free and loosely bound water and then combined with tightly bound water, inducing the increase in hydrogen bonds and molecular interactions. Therefore, the thermal transition temperature (Tt ) and storage modulus (G') obviously increased from 47.3 ± 0.5°C and 0.1 kPa to 92.7 ± 0.8°C and 7.8 kPa, respectively. Unfortunately, the high deformation (γ > 60%) and low recovery percentage (R < 15%) reflected the poor anti-deformation of gels due to the volatility of ethanol. For HGC, the entanglement and rigidity of fibrils increased owing to the contraction of cross-linked fibrils and cohesive action of denatured collagen. As a result, HGC were more resistant to deformation and exhibited more elasticity than native collagen gel, accompanied by the fact that G' and R increased to 28.8 kPa and 90.0% ± 0.7%. Additionally, HGC exhibited higher Tt (121.4 ± 0.5°C) due to lower water content and higher collagen concentration.
Keywords: collagen gel; cross-linking; dehydration; thermal stability; viscoelasticity.
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