Molecular and structural insights into skin collagen reveals several factors that influence its architecture
| Autor: | Bridget Ingham, Rafea Naffa, Gillian E. Norris, Simon F.R. Hinkley, Catherine Maidment, Meekyung Ahn |
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| Rok vydání: | 2018 |
| Předmět: |
macromolecular substances
02 engineering and technology Fibril Biochemistry Glycosaminoglycan 03 medical and health sciences Structural Biology Tensile Strength Ultimate tensile strength Microscopy Materials Testing Animals Denaturation (biochemistry) Molecular Biology 030304 developmental biology Glycosaminoglycans Skin 0303 health sciences Tear resistance integumentary system Chemistry Small-angle X-ray scattering Deer Temperature General Medicine 021001 nanoscience & nanotechnology Transmission electron microscopy Biophysics Cattle Collagen 0210 nano-technology |
| Zdroj: | International journal of biological macromolecules. 128 |
| ISSN: | 1879-0003 |
| Popis: | Although the biomechanical properties of skin and its molecular components have been extensively studied, little research has been devoted to understanding the links between them. Here, a comprehensive analysis of the molecular components of deer and cow skins was undertaken in order to understand the basis of their physical properties. These skins were chosen because they are known to be strong yet supple, exhibiting properties that have been exploited by man for centuries. Firstly, the tensile strength, tear strength and denaturation temperature of deer and cow skins were measured. Secondly, the organisation of the collagen fibrils and presence of glycosaminoglycans in each skin was investigated using polarising microscopy (PM), laser scanning confocal microscopy (LSCM), transmission electron microscopy (TEM), nuclear magnetic resonance (NMR) and small angle X-ray scattering (SAXS). Finally, amino acid, crosslink and glycosaminoglycan analyses were carried out on both skins in the study. The results of the study showed that individual physical properties such as tensile strength of the skin are derived from different combinations of biomolecular components which are reflected in collagen architecture. The "wavy" organisation of collagen fibres in deer skin was associated with a small fibril diameter, uniform glycosaminoglycan distribution and higher proportion of trivalent crosslinks. In contrast, the collagen fibrils in cow skin were large, contained a diverse glycosaminoglycan distribution and a higher proportion of tetravalent crosslinks, resulting in straight fibres. This study showed for the first time that the relationship between the structure of collagen in skin and its biomechanical functions is complex, arising from different architectural and molecular features including organisation of collagen fibres, diameters of collagen fibrils, distribution and amount of glycosaminoglycans and types and concentrations of crosslinks. |
| Databáze: | OpenAIRE |
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