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

doi:10.1016/j.biomaterials.2015.02.086

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

School of Chemistry

Research output: Contribution to journal › Article › Research › peer-review

48 Citations (Scopus)

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.

Original language	English
Pages (from-to)	127 - 136
Number of pages	10
Journal	Biomaterials
Volume	53
DOIs	https://doi.org/10.1016/j.biomaterials.2015.02.086
Publication status	Published - 2015

Access to Document

10.1016/j.biomaterials.2015.02.086

RM sElocation

Cite this

@article{a6e237fcc0944da3b1969aeba727fdc9,

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

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.",

author = "Greene, {George Wren} and Martin, {Lisandra Lorraine} and Tabor, {Richard Francis} and Agnes Michalczyk and Ackland, {Leigh M} and Roger Horn",

year = "2015",

doi = "10.1016/j.biomaterials.2015.02.086",

language = "English",

volume = "53",

pages = "127 -- 136",

journal = "Biomaterials",

issn = "0142-9612",

publisher = "Elsevier",

}

TY - JOUR

T1 - Lubricin: a versatile, biological anti-adhesive with properties comparable to polyethylene glycol

AU - Greene, George Wren

AU - Martin, Lisandra Lorraine

AU - Tabor, Richard Francis

AU - Michalczyk, Agnes

AU - Ackland, Leigh M

AU - Horn, Roger

PY - 2015

Y1 - 2015

N2 - 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.

AB - 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.

UR - http://tinyurl.com/kdu3shv

U2 - 10.1016/j.biomaterials.2015.02.086

DO - 10.1016/j.biomaterials.2015.02.086

M3 - Article

VL - 53

SP - 127

EP - 136

JO - Biomaterials

JF - Biomaterials

SN - 0142-9612

ER -