Graft 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. However, photomicrographs taken with the aid of a scanning electron microscope showed a breakdown of the fibrillar structure of the collagen within the copolymer at synthesis temperatures greater than 25 °C. The mechanical properties of the films and the cytotoxicity of the obtained copolymer samples were studied. The sample of a hybrid copolymer of collagen and PAA obtained at 60 °C has stronger mechanical properties compared to other tested samples. Its low cytotoxicity, when the monomer is removed, makes materials based on it promising in scaffold technologies.

Enzymatic 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. High molecular CC decays within the first minute, forming two low molecular fractions. The main part (~80%) falls on the fraction with a value of M_w less than 10 kDa. The initial high molecular fraction of Fn with M_w ~320–340 kDa is not completely hydrolyzed even after three days of control. The presence of low molecular fractions with M_w ~17 and M_w ~10 kDa in the solution slightly increases within an hour and noticeably increases for three days. The destruction of macromolecules of high molecular collagen to hydrolysis products appears almost completely within the first minute mainly to the polymer with M_w ~10 kDa, and enzymatic hydrolysis of fibrinogen proceeds slower than that of collagen, but also mainly to the polymer with M_w ~10 kDa. Comparative photos of the surfaces of native collagen, fibrinogen and the scaffold based on them were obtained.

Graft gelatin and poly(methyl methacrylate) copolymers were synthesized in the presence of the tributylborane—2,5-di-tert-butyl-p-benzoquinone (2,5-DTBQ) system. The molecular weight parameters and morphology of the polymer indicate that it has a cross-linked structure. Obtained data confirm the simultaneous formation of a copolymer in two ways: “grafting from” and “grafting to”. It leads to the cross-linked structure of a copolymer. This structure was not obtained for copolymers synthesized in the presence of other initiating systems: azobisisobutyronitrile; tributylborane; azobisisobutyronitrile and tributylborane; azobisisobutyronitrile, tributylborane, and 2,5-di-tert-butyl-p-benzoquinone. In these cases, the possibility of the formation of the copolymer, simultaneously in two ways, was excluded. Graft gelatin and poly(methyl methacrylate) copolymers synthesized in the presence of the tributylborane—2,5-di-tert-butyl-p-benzoquinone system are promising in terms of their use in scaffold technologies due to the three-dimensional mesh structure, providing a high regenerative potential of materials.

Polymerization of methyl methacrylate (MMA) in aqueous collagen (Col) dispersion was studied in the presence of tributylborane (TBB) and p-quinone: 2,5-di-tert-butyl-p-benzoquinone (2,5-DTBQ), p-benzoquinone (BQ), duroquinone (DQ), and p-naphthoquinone (NQ). It was found that this system leads to the formation of a grafted cross-linked copolymer. The inhibitory effect of p-quinone determines the amount of unreacted monomer, homopolymer, and percentage of grafted poly(methyl methacrylate) (PMMA). The synthesis combines two approaches to form a grafted copolymer with a cross-linked structure—“grafting to” and “grafting from”. The resulting products exhibit biodegradation under the action of enzymes, do not have toxicity, and demonstrate a stimulating effect on cell growth. At the same time, the denaturation of collagen occurring at elevated temperatures does not impair the characteristics of copolymers. These results allow us to present the research as a scaffold chemical model. Comparison of the properties of the obtained copolymers helps to determine the optimal method for the synthesis of scaffold precursors—synthesis of a collagen and poly(methyl methacrylate) copolymer at 60 °C in a 1% acetic acid dispersion of fish collagen with a mass ratio of the components collagen:MMA:TBB:2,5-DTBQ equal to 1:1:0.015:0.25.