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Structure and Properties of Cartilage Proteoglycans
- Source :
- Macromolecular Symposia, Macromolecular Symposia, Wiley-VCH Verlag, 2017, 372 (1), pp.43-50, Macromolecular Symposia, Wiley-VCH Verlag, 2017, 372 (1), pp.43-50. ⟨10.1002/masy.201700014⟩, Macromolecular Symposia, Wiley-VCH Verlag, 2017
- Publication Year :
- 2017
- Publisher :
- Wiley, 2017.
-
Abstract
- International audience; The most abundant cartilage proteoglycan is aggrecan, a bottlebrush shaped molecule that possesses over 100 glycosaminoglycan (chondroitin sulfate and keratan sulfate) chains. The side-chains are linear sulfated polysaccharides that are negatively charged under physiological conditions. Aggrecan interacts with hyaluronic acid (HA) to form large aggregates. Osmotic pressure measurements and rheological measurements are used to study the static and dynamic behavior of aggrecan assemblies at the macroscopic length scales. The microscopic properties of aggrecan solutions are determined by small angle neutron scattering, and static and dynamic light scattering (SLS and DLS). In dilute solutions aggrecan forms microgels with a diffuse boundary, composed of loosely connected clusters. The osmotic pressure of the aggrecan-HA system decreases with increasing HA content. DLS yields a relaxation rate that varies as q(3), arising from internal modes in the microgel. The relaxation rate in the solutions of the aggrecan-HA complex is slightly greater than in the pure aggrecan solution.
- Subjects :
- musculoskeletal diseases
animal structures
Materials science
Polymers and Plastics
Keratan sulfate
02 engineering and technology
010402 general chemistry
01 natural sciences
Article
Glycosaminoglycan
chemistry.chemical_compound
Dynamic light scattering
Materials Chemistry
Osmotic pressure
Chondroitin sulfate
ComputingMilieux_MISCELLANEOUS
Aggrecan
biology
Organic Chemistry
musculoskeletal system
021001 nanoscience & nanotechnology
Condensed Matter Physics
Small-angle neutron scattering
0104 chemical sciences
carbohydrates (lipids)
Crystallography
chemistry
Proteoglycan
embryonic structures
Biophysics
biology.protein
[PHYS.PHYS.PHYS-CHEM-PH]Physics [physics]/Physics [physics]/Chemical Physics [physics.chem-ph]
0210 nano-technology
Subjects
Details
- ISSN :
- 15213900 and 10221360
- Volume :
- 372
- Database :
- OpenAIRE
- Journal :
- Macromolecular Symposia
- Accession number :
- edsair.doi.dedup.....3e03acbdad5be455d5f096a2066969d0