Molecular Weight Parameters of Collagen from Different Feedstock and Dynamics of Their Change upon Enzymatic Hydrolysis by Pancreatin

Семенычева, Л. Л.; Valetova, N. B.; Chasova, Victoria; Podguzkova, M. V.; Захарычева, Н. С.; Egorikhina, Marfa N.; Astanina, M. V.; Kuznetsova, Yu. L.

doi:10.1134/s1995421220020203

Cited by 4 publications

(4 citation statements)

References 20 publications

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“…The molecular weight parameters of proteins in the process of enzymatic hydrolysis by thrombin are presented in Table 1. It was found earlier that the hydrolysis of native high molecular collagen of type I, isolated from the skin of different animals, under standard conditions in the presence of the enzyme-pancreatin proceeds at a sufficiently high rate [25].…”

Section: Resultsmentioning

confidence: 98%

“…It is not entirely clear how collagen interacts with fibrin during the formation of composite scaffolds under enzymatic hydrolysis conditions, however it is well known that thrombin hydrolyzes the bonds formed by arginine and lysine (Scheme 1) [24]. It was found earlier that the hydrolysis of native high molecular collagen of type I, isolated from the skin of different animals, under standard conditions in the presence of the enzyme-pancreatin proceeds at a sufficiently high rate [25].…”

Section: Introductionmentioning

confidence: 99%

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Enzymatic Hydrolysis of Marine Collagen and Fibrinogen Proteins in the Presence of Thrombin

et al. 2020

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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 Mw less than 10 kDa. The initial high molecular fraction of Fn with Mw ~320–340 kDa is not completely hydrolyzed even after three days of control. The presence of low molecular fractions with Mw ~17 and Mw ~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 Mw ~10 kDa, and enzymatic hydrolysis of fibrinogen proceeds slower than that of collagen, but also mainly to the polymer with Mw ~10 kDa. Comparative photos of the surfaces of native collagen, fibrinogen and the scaffold based on them were obtained.

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Section: Resultsmentioning

confidence: 98%

Section: Introductionmentioning

confidence: 99%

Enzymatic Hydrolysis of Marine Collagen and Fibrinogen Proteins in the Presence of Thrombin

et al. 2020

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“…Obviously, the enzymatic hydrolysis of proteins plays an important role in the formation of scaffolds. Previously, we have shown that during the enzymatic hydrolysis of CC, the destruction of a high molecular weight polymer to low molecular weight fragments occurs very quickly, almost within the first minute at room temperature [ 34 , 46 , 47 , 48 , 49 ]. During the enzymatic hydrolysis of CC together with fibrinogen responsible for the formation of the network structure, a scaffold is formed, which has a whole range of necessary biomimetic properties [ 36 , 37 ].…”

Section: Introductionmentioning

confidence: 99%

Photocatalytic Synthesis of Materials for Regenerative Medicine Using Complex Oxides with β-pyrochlore Structure

Семенычева

Chasova

Fukina

et al. 2023

Life

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Graft copolymerization of methyl methacrylate onto cod collagen was carried out under visible light irradiation (λ = 400–700 nm) at 20–25 °C using the RbTe1.5W0.5O6, CsTeMoO6, and RbNbTeO6 complex oxides with β-pyrochlore structure as photocatalysts. The as-prepared materials were characterized by X-ray diffraction, scanning electron microscopy, and UV-Vis diffuse reflectance spectroscopy. It was also found that RbNbTeO6 with β-pyrochlore structure was not able to photocatalyze the reaction. Enzymatic hydrolysis of the obtained graft copolymers proceeds with the formation of peptides with a molecular weight (MW) of about 20 and 10 kDa. In contrast to collagen, which decomposes predominantly to peptides with MW of about 10 kDa, the ratio of fractions with MW of about 10 kDa and 20 kDa differs much less, their changes are symbatic, and the content of polymers with MW of more than 20 kDa is about 70% after 1 h in the case of graft copolymers. The data obtained indicate that synthetic fragments grafted to the collagen macromolecule do not prevent the hydrolysis of the peptide bonds but change the rate of polymer degradation. This is important for creating network matrix scaffolds based on graft copolymers by cross-linking peptides, which are products of enzymatic hydrolysis.

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“…They were shown to differ in their amino acid sequences and degree of modification—the extent of hydroxylation or glycosylation [ 33 , 34 ]. However, only in recent years have works begun to appear in which collagens belonging to the same type have been shown to demonstrate different properties depending on the species of animal from whose tissues they have been isolated [ 35 , 36 , 37 , 38 ]. A.M. Carvalho et al [ 39 ] set forth a comparative study of type I collagen isolated from bovine skin, cod skin, and rat tails.…”

Section: Introductionmentioning

confidence: 99%

Changes in the Molecular Characteristics of Bovine and Marine Collagen in the Presence of Proteolytic Enzymes as a Stage Used in Scaffold Formation

et al. 2021

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Biopolymers, 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. Our present work aimed to identify the features of the molecular characteristics of collagens of different species origin and the changes they undergo during the enzymatic hydrolysis used for the process of scaffold formation. For this study, we used the methods of gel-penetrating chromatography, dynamic light scattering, reading IR spectra, and scanning electron microscopy. It was found that cod collagen (CC) and bovine collagen (BC) have different initial molecular weight parameters, and that, during hydrolysis, the majority of either type of protein is hydrolyzed by the proteolytic enzymes within the first minute. The differently sourced collagen samples were also hydrolyzed with the formation of two low molecular fractions: Mw ~ 10 kDa and ~20 kDa. In the case of CC, the microstructure of the final scaffolds contained denser, closely spaced fibrillar areas, while the BC-sourced scaffolds had narrow, short fibrils composed of unbound fibers of hydrolyzed collagen in their structure.

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Molecular Weight Parameters of Collagen from Different Feedstock and Dynamics of Their Change upon Enzymatic Hydrolysis by Pancreatin

Cited by 4 publications

References 20 publications

Enzymatic Hydrolysis of Marine Collagen and Fibrinogen Proteins in the Presence of Thrombin

Enzymatic Hydrolysis of Marine Collagen and Fibrinogen Proteins in the Presence of Thrombin

Photocatalytic Synthesis of Materials for Regenerative Medicine Using Complex Oxides with β-pyrochlore Structure

Changes in the Molecular Characteristics of Bovine and Marine Collagen in the Presence of Proteolytic Enzymes as a Stage Used in Scaffold Formation

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