Abstract
Collagen gels have been widely studied for applications in tissue engineering because of their biological implications. Considering their use as scaffolds for vascular tissue engineering, the main limitation has always been related to their low mechanical properties. During the process of in vitro self-assembly, which leads to collagen gelation, the size of the fibrils, their chemical interactions, as well as the resulting microstructure are regulated by three main experimental conditions: pH, ionic strength and temperature. In this work, these three parameters were modulated in order to increase the mechanical properties of collagen gels. The effects on the gelation process were assessed by turbidimetric and scanning electron microscopy analyses. Turbidity measurements showed that gelation was affected by all three factors and scanning electron images confirmed that major changes occurred at the microstructural level. Mechanical tests showed that the compressive and tensile moduli increased by four- and three-fold, respectively, compared to the control. Finally, viability tests confirmed that these gels are suitable as scaffolds for cellular adhesion and proliferation.
Highlights
According to the World Health Organization, cardiovascular diseases constitute one of the most important causes of mortality throughout the world [1]
As an alternative to improve the mechanical performances of collagen gel scaffolds without crosslinking treatments, this work aimed at tailoring and increasing the mechanical properties of collagen gels by modulating ionic strength, pH and temperature of gelation
Collagen gels prepared at different pHs, ionic strengths and set at different temperatures were evaluated by turbidity measurements, mechanical tests and scanning electron microscopy (SEM) imaging in order to assess the effects of these three factors on the process of self-assembly
Summary
According to the World Health Organization, cardiovascular diseases constitute one of the most important causes of mortality throughout the world [1]. The collagen family includes more than 20 types of extracellular proteins. All these types present the same molecular structure, i.e., a right-handed triple helix composed of three left-handed twists of α-chains, where each α-chain is a monotonously repeating sequence of amino acids (Gly-X-Y). Collagen types III and I are fibril-forming collagens and represent the major stress-bearing component of the fibrous matrices of blood vessels [9]. These collagens assemble into well-packed, highly-orientated aggregates, which present a characteristic banding pattern with a periodicity of about 70 nm (the D-period) [8]
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