Lubricin: a versatile, biological anti-adhesive with properties comparable to polyethylene glycol

Biomaterials. 2015 Jun:53:127-36. doi: 10.1016/j.biomaterials.2015.02.086. Epub 2015 Mar 12.

Abstract

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.

Keywords: Anti-adhesion; Biofouling; Lubricin; Non-specific binding; Quartz crystal microbalance; Surface treatment.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Glycoproteins / chemistry*
  • Polyethylene Glycols / chemistry*
  • Quartz Crystal Microbalance Techniques

Substances

  • Glycoproteins
  • lubricin
  • Polyethylene Glycols