Hydration-dehydration of adsorbed protein films studied by AFM and QCM-D.
The hydration-dehydration process of an adsorbed human serum albumin film has been studied using atomic force microscopy (AFM) and a quartz crystal microbalance (QCM). All measurements were performed with identically prepared protein films deposited on highly hydrophilic substrates. Both techniques are shown to be suitable for following in situ the kinetics of protein hydration, and for providing quantitative values of the adsorbed adlayer mass. The results obtained by the two methods have been compared and combined to study changes of physical properties of the films in terms of viscosity, shear, Young's modulus, density and film thickness. These properties were found to be reversible during hydration-dehydration cycles.
Lubarsky
G V
GV
Advanced Materials and Biomaterials Research Centre, School of Engineering, The Robert Gordon University, Aberdeen AB10 1FR, United Kingdom. gl30@st-andrews.ac.uk
Davidson
M R
MR
Bradley
R H
RH
D000327:Adsorption; D018625:Microscopy, Atomic Force; D011506:Proteins / Q000493:pharmacokinetics*; D014867:Water
D011506:Proteins; D014867:Water