Studies of Adsorption and Viscoelastic Properties of Proteins onto Liquid Crystal Phthalocyanine Surface Using Quartz Crystal Microbalance with Dissipation Technique

• Published in: Journal of physical chemistry. C 2008-08, Vol.112 (31), p.11822-11830
• Main Authors: Paul, Sharmistha, Paul, Deepen, Basova, Tamara, Ray, Asim K
• Format: Article
• Language: English
• Subjects: C: Surfaces, Interfaces, Catalysis
• ISSN: 1932-7447; 1932-7455
• DOI: 10.1021/jp800975t

This paper presents time-resolved adsorption behavior of lysozyme, bovine serum albumin (BSA), and immunogamma globulin (IgG) onto a liquid crystal phthalocyanine surface and concentrates on the kinetic, viscoelastic variation, interfacial hydration, and structural details obtained by quartz crystal microbalance dissipating monitoring (QCM-D) technique with the Voigt model. The rate of adsorption for lysozyme is faster than that of BSA and IgG. The Freundlich model can explain the adsorption isotherm of lysozyme, whereas an exponential growth model can describe that of BSA and IgG. Layer surface coverage has been found to increase for all three proteins with significant variation in surface packing density and viscoelastic parameters within the investigated concentration range. The adsorbed IgG and BSA form soft, water-rich multilayers with large energy dissipation. The layer viscosity and shear modulus have been found to decrease as the protein hydration increases with concentration in these cases. On the other hand, lysozyme forms a rigid, negligibly hydrated multilayer with higher values of viscosity, shear modulus. Among three proteins, IgG is found to be a good adsorbent for liquid crystal surface comparing their theoretical monolayer surface coverage.