Lubricin is a glycoprotein found in articular joints which has been recognized as being an important biological boundary lubricant molecule. Besides providing lubrication, we demonstrate, using a quartz crystal microbalance, that lubricin also exhibits anti-adhesive properties and is highly effective at preventing the non-specific adsorption of representative globular proteins and constituents of blood plasma. This impressive anti-adhesive property, combined with lubricin s ability to readily self-assemble to form dense, highly stable telechelic polymer brush layers on virtually any substrates, and its innate biocompatibility, makes it an attractive candidate for anti-adhesive and anti-fouling coatings. We show that coatings of lubricin protein are as effective as, or better than, self-assembled monolayers of polyethylene glycol over a wide range of pH and that this provides a simple, versatile, highly stable, and highly effective method of controlling unwanted adhesion to surfaces.
|Pages (from-to)||127 - 136|
|Number of pages||10|
|Publication status||Published - 2015|