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

George Wren Greene, Lisandra Lorraine Martin, Richard Francis Tabor, Agnes Michalczyk, Leigh M Ackland, Roger Horn

Research output: Contribution to journalArticleResearchpeer-review

62 Citations (Scopus)


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.
Original languageEnglish
Pages (from-to)127 - 136
Number of pages10
Publication statusPublished - 2015

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