An extensive experimental study into the relationships between tensiotrace features and surface tension of alcohols and bifunctional liquids has produced a series of empirical relationships. The use of this 'inside the rainbow' studies for pendant drops is known as optical tensiography. A series of empirical relationships discovered will enable the experimental measurement of surface tension without the correction factors that have been used since the development of the drop volume/weight method over a century ago for a restricted range of liquids. This approach offers potentially important applications in surface science and it is also suggested how these new relationships will be tested using theoretical models developed by the authors in the ongoing work. This paper provides the first experimental investigation into the commencement of the tensiotrace, a position at which optical coupling begins, which reveals measurement possibilities.
The adsorption properties of polymers are of great importance for implant studies. A better understanding of these properties can lead to improved implant materials. In this study the surface energy of different polymers was derived from contact angle measurements taken using profile analysis tensiometry (PAT) of sessile drops of water. The contact angles were measured for advancing and receding water drops on polished polymer surfaces and also on polymer surfaces modified by adsorbing protein to the surface prior to analysis of the sessile drop. The protein used was bovine serum albumin (BSA) and the surfaces were poly-methylmethacrylate (PMMA), poly-ether-ether-ketone (PEEK) and stainless steel. The polymer surfaces were also studied using atomic force microscopy (AFM). Images of the surfaces were taken in different states: rough, smooth and with albumin adsorbed. As a method to identify the proteins on the surface easier, anti-albumin antibodies with 30nm nano gold particles attached were adsorbed to the albumin on the surfaces. Using nano gold particles made the imaging more straightforward and thus made identification of the protein on the surface easier. The results from this work show the differing hydrophobicities of polymer surfaces under different conditions and a new nanotechnological method of protein identification.