Collagen stabilization using ionic liquid functionalised cerium oxide nanoparticle
| Autor: | Chandrasekar Inbasekar, N. Nishad Fathima |
|---|---|
| Rok vydání: | 2020 |
| Předmět: |
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Cerium oxide Sonication Dispersity Ionic Liquids Nanoparticle 02 engineering and technology Biochemistry Protein Structure Secondary Tendons 03 medical and health sciences chemistry.chemical_compound Differential scanning calorimetry X-Ray Diffraction Dynamic light scattering Structural Biology Spectroscopy Fourier Transform Infrared Zeta potential Animals Particle Size Rats Wistar Molecular Biology 030304 developmental biology 0303 health sciences Calorimetry Differential Scanning Protein Stability Chemistry Circular Dichroism Temperature Cerium General Medicine 021001 nanoscience & nanotechnology Chemical engineering Ionic liquid Nanoparticles Collagen 0210 nano-technology |
| Zdroj: | International Journal of Biological Macromolecules. 147:24-28 |
| ISSN: | 0141-8130 |
| Popis: | Nanoparticles owing to their size have a substantial influence on the biological behavior of collagen, thereby opening new channels to unfold the propensity of nanoparticles in terms of collagen stabilization. The present study aims to synthesize and characterize cerium oxide nanoparticles and to investigate their crosslinking efficiency on collagen. Cerium oxide nanoparticles, known biocatalysts, form an effective oxidation system due to their variable oxidation state. Ionic liquid functionalizes cerium oxide nanoparticles (IL-CONP) have been synthesis by the sonication method and characterizes using techniques such as Dynamic Light Scattering, and X-ray Diffraction. The hydrodynamic diameter, Zeta potential and polydispersity index of nanoparticles is 192.3 ± 2.14 nm, −13.76 ± 1.5 mV and 0.387, respectively. Changes in the secondary structure of collagen upon treatment with increasing concentration of IL-CONP indicate conformational modifications at the molecular level. Differential scanning calorimetry studies on rat tail tendon collagen fibers with IL-CONP indicate an increase in thermal stability of collagen from 61 to 87 °C. Thus, cerium oxide-based nanoparticle crosslinking invokes a considerable array of interest as a potential crosslinking agent for collagen. |
| Databáze: | OpenAIRE |
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