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The influence of collagen from various sources on skin parameters

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Treść / Zawartość
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Warianty tytułu
Języki publikacji
EN
Abstrakty
EN
Collagen is the main component of connective tissue – it represents 30% of total proteins in the animal body. This protein occurs in a wide range of tissues, e.g. in bone, skin, tendon, ligaments and cornea. It provides structural integrity, strength, resistance to tensile stress and elasticity. Due to its excellent biocompatibility and controlled biodegradability, collagen has found diverse application in the biomedical field such as wound dressing, drug carrier and tissue engineering. However, concerns about contamination of mammalian collagen have stimulated the search of another source of this biopolymer. Fish wastes are thought to be an attractive and safe new source of collagen. Fish and mammalian collagen differ in physical and chemical properties. The aim of this work was to examine the influence of collagen extracted from different sources (rat tail tendons, fish scales of northern pike (Esox lucius) and fish skin of Brama australis) on skin parameters such as hydration, colour, pH and skin’s barrier quality. The measurements had been taken on the skin surface before as well as after application of the collagen solutions. The most harmful effect on skin parameters was observed after application of rat tail collagen solution. Collagen extracted from scales of Esox lucius showed the most favourable effect on the skin parameters. The source of collagen has a significant influence on its effectiveness. The greatest virtues for human body were observed in the case of fish collagen extracted from Esox lucius scales.
Rocznik
Strony
14--17
Opis fizyczny
Bibliogr. 17 poz., wykr.
Twórcy
autor
  • Nicolaus Copernicus University in Torun, Faculty of Chemistry, Department of Chemistry of Biomaterials and Cosmetics, Gagarina 7, 87-100 Torun, Poland
autor
  • Nicolaus Copernicus University in Torun, Faculty of Chemistry, Department of Chemistry of Biomaterials and Cosmetics, Gagarina 7, 87-100 Torun, Poland
Bibliografia
  • [1] Cameron G.J., Alberts I.L., Laing J.H., Wess T.J.: Structure of type I and type III heterotypic collagen fibrils: an X-ray diffraction study. Journal of Structural Biology 137 (2002) 15-22.
  • [2] Gelse K., Pöschl E., Aigner T.: Collagens - structure, function, and biosynthesis. Advanced Drug Delivery Reviews 55 (2003) 1531-1546.
  • [3] Veeruraj A., Arumugam M., Ajithkumar T., Balasubramanian T.: Isolation and characterization of collagen from the outer skin of squid (Doryteuthis singhalensis). Food Hydrocolloids 43 (2015) 708-716.
  • [4] Peng Y.Y., Stoichevska V., Vashi A., Howell L., Fehr F., Dumsday G.J., Ramshaw J.A.M.: Non-animal collagens as new options for cosmetic formulation. International Journal of Cosmetic Science 37 (2015) 636-641.
  • [5] Hoppe H.J., Barlow P.N., Reid K.B.: A parallel three stranded α-helical bundle at the nucleation site of collagen triple-helix formation. FEBS Letters 344 (1994) 191-195.
  • [6] Brodsky B., Ramshaw J.A.: The collagen triple-helix structure. Matrix Biology 15 (1997) 545-554.
  • [7] Howland M.R., Corr L.T., Young S.M., Jones V., Jim S., Van Der Merwe N.J., Evershed R.P.: Expression of the dietary isotope signal in the compound‐specific δ13C values of pig bone lipids and amino acids. International Journal of Osteoarchaeology 13 (2003) 54-65.
  • [8] Hulmes D.J.: Building collagen molecules, fibrils, and suprafibrillar structures. Journal of Structural Biology 137 (2002) 2-10.
  • [9] Fratzl P.: Cellulose and collagen: from fibres to tissues. Current Opinion in Colloid & Interface Science 8 (2003) 32-39.
  • [10] P. Fratzl, Collagen: structure and mechanics, an introduction. In Collagen (pp. 1-13). Springer, Boston, MA, 2008.
  • [11] Cheng W., Yan-hua R., Fang-gang N., Guo-an Z.: The content and ratio of type I and III collagen in skin differ with age and injury. African Journal of Biotechnology 10 (2011) 2524-2529.
  • [12] Gómez-Guillén M.C., Giménez B., López-Caballero M.A., Montero M.P.: Functional and bioactive properties of collagen and gelatin from alternative sources: A review. Food Hydrocolloids 25 (2011) 1813-1827.
  • [13] Pati F., Adhikari B., Dhara S.: Isolation and characterization of fish scale collagen of higher thermal stability. Bioresource Technology 101 (2010) 3737-3742.
  • [14] Giraud-Guille M.M., Besseau L., Chopin C., Durand P., Herbage D.: Structural aspects of fish skin collagen which forms ordered arrays via liquid crystalline states. Biomaterials 21 (2000) 899-906.
  • [15] Kozlowska J., Sionkowska A., Skopinska-Wisniewska J., Piechowicz K.: Northern pike (Esox lucius) collagen: Extraction, characterization and potential application. International Journal of Biological Macromolecules 81 (2015) 220-227.
  • [16] Kozlowska J., Sionkowska A., Osyczka A.M., Dubiel M.: Stabilizing effect of carbodiimide and dehydrothermal treatment crosslinking on the properties of collagen/hydroxyapatite scaffolds. Polymer International 66 (2017) 1164-1172.
  • [17] Sionkowska A., Kozłowska J., Skorupska M., Michalska M.: Isolation and characterization of collagen from the skin of Brama australis. International Journal of Biological Macromolecules 80 (2015) 605-609.
Uwagi
Opracowanie rekordu w ramach umowy 509/P-DUN/2018 ze środków MNiSW przeznaczonych na działalność upowszechniającą naukę (2018).
Typ dokumentu
Bibliografia
Identyfikator YADDA
bwmeta1.element.baztech-138c020e-1ed9-41ed-a99c-96f09c376e71
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