Collagen is a suitable material for regenerative medicine because it is characterized by its good biocompatibility. However, due to its fibrillar structure, it cannot organize itself into three-dimensional porous structures without additional modification. The introduction of synthetic monomer elements into the collagen macromolecules is a technique used to form three-dimensional, collagen-based, branched, and crosslinked structures.
View Article and Find Full Text PDFPolymerization of methyl methacrylate (MMA) in aqueous collagen (Col) dispersion was studied in the presence of tributylborane (TBB) and -quinone: 2,5-di-tert-butyl--benzoquinone (2,5-DTBQ), -benzoquinone (BQ), duroquinone (DQ), and -naphthoquinone (NQ). It was found that this system leads to the formation of a grafted cross-linked copolymer. The inhibitory effect of -quinone determines the amount of unreacted monomer, homopolymer, and percentage of grafted poly(methyl methacrylate) (PMMA).
View Article and Find Full Text PDFGraft copolymers of collagen and polyacrylamide (PAA) were synthesized in a suspension of acetic acid dispersion of fish collagen and acrylamide (AA) in the presence of tributylborane (TBB). The characteristics of the copolymers were determined using infrared spectroscopy and gel permeation chromatography (GPC). Differences in synthesis temperature between 25 and 60 °C had no significant effect on either proportion of graft polyacrylamide generated or its molecular weight.
View Article and Find Full Text PDFBiopolymers, in particular collagen and fibrinogen, are the leading materials for use in tissue engineering. When developing technology for scaffold formation, it is important to understand the properties of the source materials as well as the mechanisms that determine the formation of the scaffold structures. Both factors influence the properties of scaffolds to a great extent.
View Article and Find Full Text PDFEnzymatic hydrolysis of native collagen and fibrinogen was carried out under comparable conditions at room temperature. The molecular weight parameters of proteins before and after hydrolysis by thrombin were monitored by gel-penetrating chromatography (GPC). An analysis of the experiment results shows that the molecular weight parameters of the initial fibrinogen (Fn) and cod collagen (CC) are very similar.
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