albumin - publications

Predict more albumin - ligand interactions now!

1. J Biomed Mater Res A. 2012 May 5. doi: 10.1002/jbm.a.34036. [Epub ahead of print]

Adhesion of Staphylococcus epidermidis to biomaterials is inhibited by
fibronectin and albumin.

Linnes JC, Mikhova K, Bryers JD.

Department of Bioengineering, University of Washington, Seattle, Washington

Decades of contradictory results have obscured the exact role of adsorbed
fibronectin in the adhesion of the bacterium, Staphylococcus epidermidis, to
biomaterials. Here, the ability of adsorbed fibronectin (FN) or bovine serum
albumin (BSA) to modulate S. epidermidis adhesion to various biomaterials is
reported. FN or BSA was adsorbed in increasing surface densities up to saturated
monolayer coverage onto various common biomaterials, including poly(ethylene
terephthalate), fluorinated ethylene propylene, poly(ether urethane), silicone,
and borosilicate glass. Despite the wide range of surface characteristics
represented, adsorption isotherms varied only subtly between materials for the
two proteins considered. S. epidermidis adhesion to the various protein-coated
biomaterials was quantified in a static-fluid batch adhesion assay. Although
slight differences in overall adherent cell numbers were observed between the
various protein-coated substrata, all materials exhibited significant
dose-dependent decreases in S. epidermidis adhesion with increasing adsorption of
either protein (FN, BSA) to all surfaces. Results here indicate that S.
epidermidis adhesion to FN-coated surfaces is not a specific adhesion (i.e.,
receptor: ligand) mediated process, as no significant difference in adhesion was
found between FN- and BSA-coated materials. Rather, results indicate that
increasing surface density of either FN or BSA actually inhibited S. epidermidis
adhesion to all biomaterials examined. © 2012 Wiley Periodicals, Inc. J Biomed
Mater Res Part A: , 2012.

Copyright © 2011 Wiley Periodicals, Inc.

PMID: 22566405 [PubMed - as supplied by publisher]