Journal article
Cartilage Aggrecan Can Undergo Self-Adhesion
Biophysical journal, v 95(10), pp 4862-4870
2008
PMCID: PMC2576402
PMID: 18676640
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
Here it is reported that aggrecan, the highly negatively charged macromolecule in the cartilage extracellular matrix, undergoes Ca
2+-mediated self-adhesion after static compression even in the presence of strong electrostatic repulsion in physiological-like solution conditions. Aggrecan was chemically end-attached onto gold-coated planar silicon substrates and gold-coated microspherical atomic force microscope probe tips (end radius
R
≈
2.5
μm) at a density (∼40
mg/mL) that simulates physiological conditions in the tissue (∼20–80
mg/mL). Colloidal force spectroscopy was employed to measure the adhesion between opposing aggrecan monolayers in NaCl (0.001–1.0
M) and NaCl
+
CaCl
2 ([Cl
−]
=
0.15
M, [Ca
2+]
=
0 – 75
mM) aqueous electrolyte solutions. Aggrecan self-adhesion was found to increase with increasing surface equilibration time upon compression (0–30
s). Hydrogen bonding and physical entanglements between the chondroitin sulfate-glycosaminoglycan side chains are proposed as important factors contributing to aggrecan self-adhesion. Self-adhesion was found to significantly increase with decreasing bath ionic strength (and hence, electrostatic double-layer repulsion), as well as increasing Ca
2+ concentration due to the additional ion-bridging effects. It is hypothesized that aggrecan self-adhesion, and the macromolecular energy dissipation that results from this self-adhesion, could be important factors contributing to the self-assembled architecture and integrity of the cartilage extracellular matrix in vivo.
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Details
- Title
- Cartilage Aggrecan Can Undergo Self-Adhesion
- Creators
- Lin Han - Massachusetts Institute of TechnologyDelphine Dean - Massachusetts Institute of TechnologyLaura A. Daher - Massachusetts Institute of TechnologyAlan J. Grodzinsky - Massachusetts Institute of TechnologyChristine Ortiz - Massachusetts Institute of Technology
- Publication Details
- Biophysical journal, v 95(10), pp 4862-4870
- Publisher
- Elsevier
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- School of Biomedical Engineering, Science, and Health Systems
- Web of Science ID
- WOS:000260519300037
- Scopus ID
- 2-s2.0-58149299895
- Other Identifier
- 991019187086804721
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- Web of Science research areas
- Biophysics