Adsorption of plasma proteins on hydrophobic surfaces. IV. Contact angle studies on implanted polymers

✍ Scribed by Bagnall, R. D. ;Annis, J. A. D. ;Sherliker, S. J.

• Publisher: John Wiley and Sons
• Year: 1980
• Tongue: English
• Weight: 530 KB
• Volume: 14
• Category: Article
• ISSN: 0021-9304
• DOI: 10.1002/jbm.820140102

✦ Synopsis

Abstract

Contact angle studies have been carried out on plasma protein layers adsorbed on selected polymer surfaces under buffered saline at 37°, in an attempt to demonstrate directly a recent suggestion that the interfacial free energy between such protein layers and surrounding liquid phase should be zero at equilibrium. Although an initial contact angle of 180° was always obtained, the angle decayed slowly to a stationary value which varied for any one drop on each polymer surface. The stationary values could be reasonably correlated with the reversible work of adhesion predicted for each polymer/protein combination, suggesting that protein desorption from the solid surface is a dominant event in the contact angle decay process. It is concluded that the data bear more relevance to the protein layer/polymer interface than to the protein layer/solution interface, and that the contact angle technique is not a suitable technique for studying the latter on biomaterials.