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Beilstein Journal of Nanotechnology (1)
Journal of biomechanics (1)
Soft matter (1)
Zauscher, Stefan (3)
Chang, Debby P. (2)
Guilak, Farshid (2)
Abu-Lail, Nehal I. (1)
Chang, Debby P (1)
Chen, Tao (1)
Coles, Jeffrey M. (1)
Jay, Gregory (1)
Jay, Gregory D. (1)
Jordan, Rainer (1)
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author:("Chang, derby P")
Interaction of Lubricin with Collagen II Surfaces: Adsorption, Friction, and Normal Forces
Journal of biomechanics
One of the major constituents of the synovial fluid that is thought to be responsible for chondroprotection and boundary lubrication is the glycoprotein lubricin (PRG4); however, the molecular mechanisms by which lubricin carries out its critical functions still remain largely unknown. We hypothesized that the interaction of lubricin with type II collagen, the main component of the cartilage extracellular matrix, results in enhanced tribological and wear properties. In this study, we examined: i) the molecular details by which lubricin interacts with type II collagen and how binding is related to boundary lubrication and adhesive interactions; and, ii) whether collagen structure can affect lubricin adsorption and its chondroprotective properties. We found that lubricin adsorbs strongly onto denatured, amorphous, and fibrillar collagen surfaces. Furthermore, we found large repulsive interactions between the collagen surfaces in presence of lubricin, which increased with increasing lubricin concentration. Lubricin attenuated the large friction and also the long-range adhesion between fibrillar collagen surfaces. Interestingly, lubricin adsorbed onto and mediated the frictional response between the denatured and native amorphous collagen surfaces equally and showed no preference on the supramolecular architecture of collagen. However, the coefficient of friction was lowest on fibrillar collagen in the presence of lubricin. We speculate that an important role of lubricin in mediating interactions at the cartilage surface is to attach to the cartilage surface and provide a protective coating that maintains the contacting surfaces in a sterically repulsive state.
Colloidal Probe Microscopy; Lateral Force Microscopy; Atomic Force Microscope; Friction; Tribology; PRG4; Wear; Glycoproteins; Collagen; Type II Collagen Lubricin; SAMs; Boundary Lubrication
Colloidal lithography for fabricating patterned polymer-brush microstructures
Beilstein Journal of Nanotechnology
We exploit a series of robust, but simple and convenient colloidal lithography (CL) approaches, using a microsphere array as a mask or as a guiding template, and combine this with surface-initiated atom-transfer radical polymerization (SI-ATRP) to fabricate patterned polymer-brush microstructures. The advantages of the CL technique over other lithographic approaches for the fabrication of patterned polymer brushes are (i) that it can be carried out with commercially available colloidal particles at a relatively low cost, (ii) that no complex equipment is required to create the patterned templates with micro- and nanoscale features, and (iii) that polymer brush features are controlled simply by changing the size or chemical functionality of the microspheres or the substrate.
atom-transfer radical polymerization; colloidal lithography; patterning; self-assembled microsphere monolayer
Friction Force Microscopy of Lubricin and Hyaluronic Acid between Hydrophobic and Hydrophilic Surfaces
Abu-Lail, Nehal I.
Coles, Jeffrey M.
Jay, Gregory D.
Lubricin and hyaluronic acid (HA), molecular constituents of synovial fluid, have long been theorized to play a role in joint lubrication and wear protection. While lubricin has been shown to function as a boundary lubricant, conflicting evidence exists as to the boundary lubricating ability of hyaluronic acid. Here, we use colloidal force microscopy to explore the friction behavior of these two molecules on the microscale between chemically uniform hydrophilic (hydroxyl-terminated) and hydrophobic (methyl-terminated) surfaces in physiological buffer solution. Behaviors on both surfaces are physiologically relevant since the heterogeneous articular cartilage surface contains both hydrophilic and hydrophobic elements. Friction between hydrophobic surfaces was initially high (μ=1.1, at 100nN of applied normal load) and was significantly reduced by lubricin addition while friction between hydrophilic surfaces was initially low (μ=0.1) and was slightly increased by lubricin addition. At lubricin concentrations above 200 µg/ml, friction behavior on the two surfaces was similar (μ=0.2) indicating that nearly all interaction between the two surfaces was between adsorbed lubricin molecules rather than between the surfaces themselves. In contrast, addition of HA did not appreciably alter the frictional behavior between the model surfaces. No synergistic effect on friction behavior was seen in a physiological mixture of lubricin and HA. Lubricin can equally mediate the frictional response between both hydrophilic and hydrophobic surfaces, likely fully preventing direct surface-to-surface contact at sufficient concentrations, whereas HA provides considerably less boundary lubrication.
Colloidal force microscopy; Lateral force microscopy; Atomic force microscope; Friction; Tribology; PRG4; Wear; Glycoproteins; Hyaluronic acid; Lubricin; Joint lubrication; Cartilage lubrication; Self-assembled monolayer; Synovial lubricants
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