Kuntala Banerjee , Sreesaila S , T Hemalatha , N. Nishad Fathima
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引用次数: 0
Abstract
The self-assembly of collagen in vitro differs from in vivo mainly in packing densities, mechanical strength, diameter and porosity depending on pH and temperature. The use of collagen in biomedical and pharmaceutical industry necessitates the need for tuned-assembly of collagen and understanding the mechanical and chemical properties of the tuned collagen-fibrils. In this study, we have focused on non-toxic crosslinking of collagen by introducing asarylaldehyde, a compound found in carrot seed, into the fibrillation process of type-I collagen and explored the mechanical and chemical properties of that tuned assembly. Upon interaction of collagen with asarylaldehyde, the fibrillisation process accelerated and showed highest rate of fibril formation at 1:100 molar-ratio. The tuned assembly shows thixotropy and LVR is increased up to 1:25 molar-ratio compared to native fibrils. The fibril diameter is increased and D-periodicity is decreased for 1:100 molar-ratio as observed through SEM images. The negative Gibbs free energy and binding constant values confirm there is a strong binding attraction between tropocollagen and the asarylaldehyde molecule. MTT assay and fluorescence staining displayed the biocompatible nature of the prepared scaffold. The known cell proliferation as well as bone metabolism properties of asarylaldehyde may value-add the prepared scaffold for tissue engineering applications.
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