Collagen - structure, properties and application

• Autorzy: Owczarzy Aleksandra , Kurasiński Robert , Kulig Karolina , Rogóż Wojciech , Szkudlarek Agnieszka , Maciążek-Jurczyk Małgorzata

Identyfikatory

DOI

10.34821/eng.biomat.156.2020.17-23

• Języki publikacji: EN

Abstrakty

EN

Collagen is the dominant component of the extracellular matrix of mammals. It occurs almost in all animal tissues. Collagen is a highly heterogeneous protein. The collagen protein family is characterized by great diversity in terms of structure, occurrence, and function. Up till now, 29 types of collagens proteins have been classified. The representation of individual types of collagen has certain common features. The most important property is the above-average mechanical strength that results directly from the spatial structure. Collagen is a building material for most tissues and organs. It also plays an important role in the process of cell growth and differentiation, which results from the specific structure of collagen fibers as well as their ability to adhere. The development of research techniques allowed to study in detail the molecular structure and properties of collagen. Therefore, collagen has become a subject of interest in many branches of science. Synthetic recombinant collagen fibers were developed as the basis of collagen biomaterials for medical applications, including implantology or gynecology. The specific structure of collagen also makes it applicable as a protein carrier in drug delivery systems (DDS), particularly in the treatment of cancer and genetic diseases. The use of tissue regenerative abilities and an interdisciplinary look at the properties of collagen and collagen-based biomaterials may constitute the future of medical development.

Słowa kluczowe

EN

collagen; collagen structure; physicochemical properties; biological properties; DDS; physicochemical techniques; atelocollagen

• Wydawca: Polish Society for Biomaterials in Cracow
• Czasopismo: Engineering of Biomaterials
• Rocznik: 2020
• Tom: Vol. 23, no. 156
• Strony: 17--23
• Opis fizyczny: Bibliogr. 47 poz., rys., tab.

Twórcy

autor

Owczarzy Aleksandra

• Department of Physical Pharmacy, Faculty of Pharmaceuticals Sciences in Sosnowiec, Medical University of Silesia in Katowice, ul. Jagiellońska 4, 41-200 Sosnowiec, Poland

autor

Kurasiński Robert

• Cardiology Center, Szpitalna 1, 41-219 Sosnowiec, Poland

autor

Kulig Karolina

• Department of Physical Pharmacy, Faculty of Pharmaceuticals Sciences in Sosnowiec, Medical University of Silesia in Katowice, ul. Jagiellońska 4, 41-200 Sosnowiec, Poland

autor

Rogóż Wojciech

• Department of Physical Pharmacy, Faculty of Pharmaceuticals Sciences in Sosnowiec, Medical University of Silesia in Katowice, ul. Jagiellońska 4, 41-200 Sosnowiec, Poland

autor

Szkudlarek Agnieszka

• Department of Physical Pharmacy, Faculty of Pharmaceuticals Sciences in Sosnowiec, Medical University of Silesia in Katowice, ul. Jagiellońska 4, 41-200 Sosnowiec, Poland

autor

Maciążek-Jurczyk Małgorzata

• Department of Physical Pharmacy, Faculty of Pharmaceuticals Sciences in Sosnowiec, Medical University of Silesia in Katowice, ul. Jagiellońska 4, 41-200 Sosnowiec, Poland

Bibliografia

• [1] Meyer M.: Processing of collagen based biometrerials and the resulting materials properties. BioMedical Engineering OnLine (2019)
• [2] Morąg M., Burza A.: Budowa, właściwości i funkcje kolagenu oraz elastyny w skórze. Journal of Health Study and Medicine 2 (2017) 77-100.
• [3] Birk D.E., Bruckner P.: Collagen Suprastructures. Collagen. Springer (2015) 185-205.
• [4] Brodsky B. Ramshaw J.: The collagen Triple – Helix Structure. Matrix Biology (1997) 545-554.
• [5] Wagenaar-Miller R., Engelholm L., Gavard J., et al.: Complementary Roles of Intracellular and Pericellular, Collagen Degradation Pathways In Vivo. Molecular and Cellular Biology (2007) 6309-6322.
• [6] Burjanadze T.V.: New analysis of the Phylogenetic Change of Collagen Thermostability. Biopolymers 53 (2000) 523-528.
• [7] Domene C., Jorgensen C., Wajid Abbasi S.: A perspective on structural and computational work on collagen. Physical Chemistry Chemical Physics 18 (2016) 24802-24811.
• [8] Czubak K., Żbikowska H.: Struktura, funkcja i znaczenie biomedyczne kolagenów. Annales Academiae Medicae Silesiensis 68 (2014) 245-254.
• [9] Shoulders M., Raines R.: Collagen Structure and Stability. Annual Review of Biochemistry 78 (2009) 929-958.
• [10] Brodsky B., Persikov A.: Molecular structure of the collagen triple helix. Advanced in Protein Chemistry 70 (2005) 301-339.
• [11] Ricard-Blum S.: The Collagen Family. Cold Spring Harbor Perspectives in Biology (2011) 1-19.
• [12] Sorushanova A., Delgado L., Wu Z., et al.: The Collagen Suprafamily: From Biosynthesis to Advanced Biomaterial Development. Advanced Materials 31 (2019) 1801651.
• [13] Gelse K., Pöschl E., Aigner T.: Collagens – structure, function, and biosynthesis. Advanced Drug Delivery Reviews 55 (2003) 1531-1546.
• [14] Holmes D., Lu Y., Starborg T., et al.: Collagen Fibril Assembly and Function. Current Topics in Developmental Biology 130 (2018) 107-142.
• [15] Mienaltowski M.J., Birk D.E.: Structure, physiology, and biochemistry of collagens. Advances in Experimental Medicine and Biology 802 (2014) 5-29.
• [16] Granner D.K.: Synteza białek i kod genetyczny. Biochemia Harpera, Murray RK, Granner DK, Mayes PA, Rodwell V. W. Wydawnictwo Lekarskie PZWL (1995) 491-507.
• [17] Sprangers S., Everts V.: Molecular pathways of cell-mediated degradation of fbrillar collagen. Matrix Biology 2017.
• [18] McKleroy W., Lee T.H., Atabai K.: Always cleave up your mess: targeting collagen degradation to treat tissue fibrosis. American Journal Of Physiology Lung Cellular and Molecular Physiology. 304 (2013) 709-721.
• [19] Strzyż P.: Collagen around the clock. Nature Review Molecular Cell Biology (2020)
• [20] Gauza M., Kubisz L., Przybylski J.: Właściwości preparatów kolagenowych ze skór ryb pozyskiwanych metodą kwaśnej hydratacji. Nowiny Lekarskie 79 (2010) 157-162.
• [21] Engel J.: Investigation of the Denaturation and Renaturation of Soluble Collagen by Light Scattering. Archives of Biochemistry and Biophysics 97 (1962) 150-158.
• [22] Harkness R.: Biological functions of collagen. Biological review 36 (1961) 399-463.
• [23] Wahyudi H., Reynolds A.A., Li Y., et al.: Targeting collagen for diagnostic imaging and therapeutic delivery. Journal of Controlled Release 240 (2016) 323-331.
• [24] Jikko A., Harris S.E., Chen D., et al.: Collagen Integrin Receptors Regulate Early Osteoblast Differentiation Induced by BMP-2. Journal of Bone and Mineral Research 14 (1999) 1075-1083.
• [25] Fang M., Yuan J., Peng Ch., Li Y.: Collagen as a double-edged sword in tumour progression. Tumour Biology 35 (2014) 2871-2882.
• [26] Jokinen J., Dado E., Nykvist P., et al.: Integrin – mediated Cell Adhesion to Type I Collagen Fibrils. The Journal of Biological Chemistry 279 (2004) 31956-31963.
• [27] Ruggeri A., Benazzo F.: Collagen – proteoglycan interaction. Ultrastructure of the Connective Tissue Matrix. Electron Microscopy in Biology and Medicine book series (1984) 113-125.
• [28] Broom N., Silyn-Roberts H.: Collagen – Collagen Versus Collagen Proteoglycan Interactions in the Determination of Cartilage Strength. Arthritis & Rheumatology 33 (1990) 1512-1517.
• [29] Burkhardt H., Sehnert B., Bockermann R., et al.: Humoral immune response to citrullinated collagen type II determinants in early rheumatoid arthritis. European Journal of Immunology 35 (2005) 1643-1652.
• [30] Krieger M., Herz J.: Structures and Functions of multiligand lipoprotein receptors and LDL Receptor – Related Protein (LRP). Annual Review of Biochemistry 63 (1994) 601-637.
• [31] Gobeaux F., Mosser G., Anglo A., et al.: Fibrillogenesis in dense collagen solutions: a physicochemical study. Journal of Molecular Biology 376 (2008) 1509-1522.
• [32] Besseau L., Giraud-Guille M. M.: Stabilization of fluid cholesteric phases of collagen to ordered gelated matrices. Journal of Molecular Biology 251 (1995) 197-202.
• [33] An B., Lin Y., Brodsky B.: Collagen interactions: Drug design and delivery. Advanced Drug Delivery Reviews. 97 (2016) 69-84.
• [34] Chattopadhyay S., Raines R.: Collagen – Based Biomaterials for Wound Healing, Biopolymers 101 (2014) 821-833.
• [35] Turek A., Kasperczyk J., Dzierżewicz Z.: Zastosowanie kolagenu w technologii postaci leku. Osiągnięcia i perspektywy. Chemik 64 (2010) 1-5.
• [36] Lynn A.K., Yannas I.V., Bonfield W.: Antigenicity and immunogenicity of collagen. Journal of Biomedical Materials Research 71 (2004) 343-354.
• [37] Lee C.H., Singla A., Lee Y.: Biomedical applications of collagen. International Journal of Pharmaceutics 221 (2001) 1-22.
• [38] Wysocki T., Sacewicz I., Wiktorska M., et al.: Atelokolagen jako potencjalny nośnik terapeutyków. Postępy Higieny i Medycyny Doświadczalnej 61 (2007) 646-654.
• [39] Nevozhay D., Kańska U., Budzyńska R., et al.: Współczesny stan badań nad koniugatami i innymi systemami dostarczania leków w leczeniu schorzeń nowotworowych i innych jednostek chorobowych. Postępy Higieny i Medycyny Doświadczalnej 61 (2007) 350-360.
• [40] Zhang Z., Guoying L., Shi B.: Physicochemical Properties of Collagen, Gelatin and Collagen Hydrolysate Derived from Bovine Limed Split Wastes. Journal of the Society of Leather Technologists and Chemists 90 (2006) 23-28.
• [41] Miles C., Avery N., Rodin V., et al.: The increase in denaturation temperature following cross – linking of collagen is caused by dehydration of the fibres. Journal of Molecular Biology 346 (2005) 551-556.
• [42] Jenness D., Sprecher C., Johnson Jr W.: Circular Dichroism of Collagen, Gelatin, and PolY(proline) II on in the Vacuum Ultraviolet. Biopolymers 15 (1976) 513-521.
• [43] Bhatnagar R.S., Gough C.A.: Circular Dichroism of Collagen and Related Polypeptides: Circular Dichroism and the Conformational Analysis of Biomolecules. Protein Science (1996) 183-199.
• [44] Du J., Long R.G., Nakai T., et al.: Functional cell phenotype induction with TGF-β1 and collagen-polyurethane scaffold for annulus fibrosus rupture repair. European Cell & Material 39 (2020) 1-17.
• [45] Harston A., Nyland J., Brand E., et al.: Collagen meniscus implantation: a systematic review including rehabilitation and return to sports activity. Knee Surgery, Sports Traumatology, Arthroscopy 20 (2012) 135-146.
• [46] Tang S.S., Mohad V., Gowda M., Thibeault S.L.: Insights Into the Role of Collagen in Vocal Fold Health and Disease. Journal of Voice 31 (2017) 520-527.
• [47] Goldberga I., Li R., Duer M.J.: Collagen Structure−Function Relationships from Solid-State NMR Spectroscopy. Accounts of Chemical Research 51 (2018) 1621-1629.

Uwagi

Opracowanie rekordu ze środków MNiSW, umowa Nr 461252 w ramach programu "Społeczna odpowiedzialność nauki" - moduł: Popularyzacja nauki i promocja sportu (2020).