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Characteristic of fish collagen films cross-linked with glutaraldehyde

Treść / Zawartość
Warianty tytułu
Języki publikacji
EN
Abstrakty
EN
Collagen is a valuable biopolymer in many fields, especially in biomedical sciences. Thanks to its biodegradability and high biocompatibility, it is a desirable material for applications that require contact with the human body. There are many sources of collagen, of which marine-origin collagen has become an important one in recent times. Pure collagen has poor stability and is sensitive to the effects of heat and other external factors. The cross-linking process can improve the properties of collagen materials. Many different methods of cross-linking can be distinguished, including chemical ones. In this study, we were concerned to obtain collagen films modified with glutaraldehyde (GTA). The influence of this additive on the chemical, mechanical, swelling, and hydrophilic properties of the biopolymeric matrix was evaluated. Two different concentrations of collagen were used, as well as three different concentrations of GTA. Results of the analysis showed that the properties of the obtained films were affected by the addition of even a small amount of cross-linker. Spectroscopic measurements indicated minor changes that reflect interactions between GTA and the collagen matrix. Mechanical tests showed changes for modified samples in values of tensile strength, breaking force, and elongation at break. The hydrophilicity decreased slightly for films with GTA. The durability of the modified samples in the swelling test increased. Differences between 1% and 2% collagen films with additives were also observed. The GTA-obtained fish collagen films can be promising materials for biomedical applications.
Rocznik
Strony
25--32
Opis fizyczny
Bibliogr. 24 poz., tab., wykr., zdj.
Twórcy
  • Department of Chemistry of Biomaterials and Cosmetics, Nicolaus Copernicus University in Toruń, ul. Gagarina 7, 87-100 Toruń, Poland
  • Department of Chemistry of Biomaterials and Cosmetics, Nicolaus Copernicus University in Toruń, ul. Gagarina 7, 87-100 Toruń, Poland
  • Department of Chemistry of Biomaterials and Cosmetics, Nicolaus Copernicus University in Toruń, ul. Gagarina 7, 87-100 Toruń, Poland
  • Department of Chemistry of Biomaterials and Cosmetics, Nicolaus Copernicus University in Toruń, ul. Gagarina 7, 87-100 Toruń, Poland
  • SanColl Sp. z o.o., ul. Juliusza Słowackiego 24, 35-060 Rzeszów, Poland
Bibliografia
  • [1] Chen X., Zhou L., Xu H., Yamamoto M., Shinoda M., Kishimoto M., Tanaka T., Yamane H.: Effect of the Application of a Dehydrothermal Treatment on the Structure and the Mechanical Properties of Collagen Film. Materials 13 (2020) 377.
  • [2] Bose S., Li S., Mele E., Williams C.J., Silberschmidt V.V.: Stability and mechanical performance of collagen films under different environmental conditions. Polymer Degradation and Stability 197 (2022) 109853.
  • [3] Adamiak K., Sionkowska A.: Current methods of collagen cross-linking: Review. International Journal of Biological Macromolecules 161 (2020) 550-560.
  • [4] Hwang S.J., Kim S.H., Seo W.-Y., Jeong Y., Shin M.C., Ryu D., Lee B. S., Choi Y.J., Kim K.: Effects of human collagen α-1 type I-derived proteins on collagen synthesis and elastin production in human dermal fibroblasts. BMB Reports 54 (2021) 329-334.
  • [5] Sionkowska A., Musiał K., Gadomska M., Adamiak K.: Fish collagen and chitosan mixtures as a promising biomaterial for potential use in biomedicine and cosmetic industry. Engineering of Biomaterials 164 (2022) 16-24.
  • [6] Sionkowska A., Adamiak K., Musiał K., Gadomska M.: Collagen Based Materials in Cosmetic Applications: A Review. Materials 13 (2020) 4217.
  • [7] Reilly D.M., Lozano J.: Skin collagen through the lifestages: importance for skin health and beauty. Plastic and Aesthetic Research 8 (2021) 2.
  • [8] Darvish M.D.: Collagen fibril formation in vitro: From origin to opportunities. Materials Today Bio 15 (2022) 100322.
  • [9] Davison-Kotler E., Marshall W.S., Garcia-Gareta E.: Sources of Collagen for Biomaterials in Skin Wound Healing. Bioengineering 6 (2019) 56.
  • [10] Silvipriya K.S., Kumar K.K., Bhat A.R., Kumar D.B., John A., Iakshamanan P.: Collagen: Animal Sources and Biomedical Application. Journal of Applied Pharmaceutical Science 5 (2015) 123-127.
  • [11] Leon-Lopez A., Morales-Penaloza A., Martinez-Juarez V.M., Vargas-Torres A., Zeugolis D.I., Alvarez-Aguirre G.: Hydrolyzed Collagen – Sources and Applications. Molecules 24 (2019) 4031.
  • [12] Nunez S.M., Guzman F., Valencia P., Almonacid S., Cardenas C.: Collagen as a source of bioactive peptides: A bioinformatics approach. Electronic Journal of Biotechnology 48 (2020) 101-108.
  • [13] Felician F.F., Xia C., Qi W., Xu H.: Collagen from Marine Biological Sources and Medical Applications. Chemistry & Biodiversity 15(5) (2018) 1700557.
  • [14] Blanco M., Vazquez J.A., Perez-Martin R.I., Sotelo C.G.: Hydrolysates of Fish Skin Collagen: An Opportunity for Valorizing Fish Industry Byproducts. Marine Drugs 15 (2017) 131.
  • [15] Gallo N., Natali M.L., Quarta A., Gaballo A., Terzi A., Sibillano T., Giannini C., Benedetto G.E., Lunetti P., Capobianco L., Blasi F.S., Sicuro A., Corallo A., Sannino A., Salvatore L.: Aquaponics-Derived Tilapia Skin Collagen for Biomaterials Development. Polymers 14 (2022) 1865.
  • [16] Dong Y., Dai Z.: Physicochemical, Structural and Antioxidant Properties of Collagens from the Swim Bladder of Four Fish Species. Marine drugs 20 (2022) 550.
  • [17] Sionkowska A., Lewandowska K., Adamiak K.: The influence of uv light on rheological properties of collagen extracted from silver carp skin. Materials 13 (2020) 4453.
  • [18] Islam M.M., AbuSamra D.B., Chivu A., Argueso P., Dohlman C.H., Patra H.K., Chodosh J., Gonzales-Andrades M.: Optimization of Collagen Chemical Crosslinking to Restore Biocompatibility of Tissue-Engineering Scaffolds. Pharmaceutics 13 (2021) 832.
  • [19] Nair M., Calahorra Y., Kar-Narayan S., Best S.M., Cameron R.E.: Self-assembly of collagen bundles and enhanced piezoelectricity induced by chemical crosslinking. Nanoscale 11 (2019) 15120.
  • [20] Peng Y.Y., Glattauer V., Ramshaw J.A.M.: Stabilisation of Collagen Sponges by Glutaraldehyde Vapour Crosslinking. International Journal of Biomaterials 2017 (2017) 1-6.
  • [21] Damink L.H.H.O., Dijkstra P.J., Luyn M.J.A., Wachem P.B., Nieuwenhuis P., Feijen J.: Glutaraldehyde as a crosslinking agent for collagen-based biomaterials. Journal of Materials Science: Materials in Medicine 6 (1995) 460-472.
  • [22] Slimane E.B., Sadok S.: Collagen from Cartilagious Fish By-Products for a Potential Application in Bioactive Film Composite. Marine Drugs 16 (2018) 211.
  • [23] Sionkowska A., Wiśniewski M., Skopińska J., Mantovani D.: Effects of Solar Radiation on Collagen-Based Biomaterials. International Journal of Photoenergy 2006 (2006) 1-6.
  • [24] Elango J., Bu Y., Bin B., Geevaretnam J., Robinson J.S., Wu W.: Effect of chemical and biological cross-linkers on mechanical and functional properties of shark catfish skin collagen films. Food Bioscience 17 (2017) 42-51.
Uwagi
Opracowanie rekordu ze środków MEiN, umowa nr SONP/SP/546092/2022 w ramach programu „Społeczna odpowiedzialność nauki” - moduł: Popularyzacja nauki i promocja sportu (2022-2023)
Typ dokumentu
Bibliografia
Identyfikator YADDA
bwmeta1.element.baztech-9864379c-de8c-4ae5-a5b6-ad77e4012bc4
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