Denaturation processes of collagen from cow bones as a function of temperature
| Autor: | Enrique David Victor Giordano, Osvaldo Agustin Lambri, Griselda Irene Zelada, Damián Gargicevich, Federico Guillermo Bonifacich, Patricia Beatriz Bozzano, Melania Lucila Lambri |
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| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
BONE REPAIR COW BONES General Physics and Astronomy INGENIERÍAS Y TECNOLOGÍAS 02 engineering and technology law.invention 03 medical and health sciences law Ingeniería de los Materiales medicine General Materials Science Denaturation (biochemistry) ARCHAEOMETRY Crystallization Rib cage Chemistry Cartilage General Chemistry Dynamic mechanical analysis Compuestos TISSUE ENGINEERING 021001 nanoscience & nanotechnology Random coil 030104 developmental biology medicine.anatomical_structure purl.org/becyt/ford/2 [https] THERMAL DENATURATION Biophysics purl.org/becyt/ford/2.5 [https] 0210 nano-technology Type I collagen Triple helix |
| Zdroj: | Matéria (Rio de Janeiro) v.23 n.2 2018 Matéria (Rio de Janeiro. Online) instacron:RLAM Matéria (Rio de Janeiro), Volume: 23, Issue: 2, Article number: e12089, Published: 19 JUL 2018 CONICET Digital (CONICET) Consejo Nacional de Investigaciones Científicas y Técnicas instacron:CONICET |
| ISSN: | 1517-7076 |
| DOI: | 10.1590/s1517-707620180002.0424 |
| Popis: | The thermal stability of collagen is of great interest for the scientific communities both of medicine and archaeology. In medicine, the interest is focused to the reconstruction and repair of bone and cartilage, given the frequency and importance of pathological situations. In contrast, in archaeology the interest is focused to infer from buried and/or burned bones the behavior and habits of people who once inhabited archaeological sites. In bones from cow ribs, the biodegradation of collagen by denaturation of albumin and haemoglobin proteins, the loss of water and the loss of crystallization water during warming up to around 450 K, have been studied. In addition, from an easy-to-handle mathematical viscoelastic procedure, it was determined that the conformational changes from the collagenic triple helix towards the random coil are made through the viscous movement of fibrils, invoking an activation energy of (127 ± 8) kJ/mol. In the present work, the thermal stability of type I collagen from cow bones, either femur and rib, was studied in the temperature range from 250 K up to 670 K by means of dynamic mechanical analysis, scanning electron microscopy and infrared absorption spectroscopy. In fact, this temperature range is wider than the previous explored ones. Several stages of denaturation were found in the temperature range from 320 K up to 670 K, including also the transition from the triple helix (TH) towards the random coil (RC) of the collagen fibrils. The temperature for the TH → RC transition was approximately the same for all the kinds of bones, but the intensity of the relaxation processes depended upon the kind of bone. The differences between the denaturation processes in the femur and rib are highlighted and the physical-chemical mechanisms controlling the denaturation processes are discussed. In fact, different behaviours of the mesostructure were found between the cortical parts of bones from ribs and femurs. In addition, the cancellous parts from ribs bone exhibits the survival of organic compounds even at temperatures as higher as 673 K. The results from the present work are crucial both for the tissue engineering, focused to bone replacement and pathologic treatments, and for the archaeology, for the study of identification of buried and/or burned bones in archaeological sites. Fil: Lambri, Melania Lucila. Universidad Nacional de Rosario. Facultad de Ciencias Exactas, Ingeniería y Agrimensura; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Bozzano, Patricia Beatriz. Comisión Nacional de Energía Atómica; Argentina Fil: Giordano, Enrique David Victor. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Procesos Biotecnológicos y Químicos Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Procesos Biotecnológicos y Químicos Rosario; Argentina Fil: Bonifacich, Federico Guillermo. Universidad Nacional de Rosario. Facultad de Ciencias Exactas, Ingeniería y Agrimensura; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Gargicevich, Damian. Universidad Nacional de Rosario. Facultad de Ciencias Exactas, Ingeniería y Agrimensura; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Zelada, Griselda Irene. Universidad Nacional de Rosario. Facultad de Ciencias Exactas, Ingeniería y Agrimensura; Argentina Fil: Lambri, Osvaldo Agustin F.. Universidad Nacional de Rosario; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina |
| Databáze: | OpenAIRE |
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