Fabrication of switchable protein resistant and adhesive multilayer membranes

• Published in: Colloids and surfaces, B, Biointerfaces B, Biointerfaces, 2012-06, Vol.94, p.118-124
• Main Authors: Mathew, Jissy, Sreedhanya, S., Baburaj, M.S., Aravindakumar, C.T., Aravind, U.K.
• Format: Article
• Language: English
• Subjects: Adhesives; Adsorption; Animals; Biocompatible Materials - chemical synthesis; BSA; Cattle; Chitosan - chemistry; Diffusion; Hydrogen-Ion Concentration; Immobilized Proteins; Lysozyme; Membranes, Artificial; Microscopy, Atomic Force; Microscopy, Electron, Scanning; Multilayers; Muramidase - chemistry; Polystyrenes - chemistry; Protein immobilization; Protein repellence; Protein Structure, Secondary; Serum Albumin, Bovine - chemistry; Sodium Chloride - chemistry; Spectroscopy, Fourier Transform Infrared; Surface Properties; Ultrafiltration
• ISSN: 0927-7765; 1873-4367
• DOI: 10.1016/j.colsurfb.2012.01.025

[Display omitted] ► Non synthetic route for the fabrication of protein adhesive/repellence surfaces. ► Pressure driven process can be utilized for the creation of protein switchable surface. ► Layer dependent adhesive/repellence polyelectrolyte multilayers on polymer support. Fabrication of protein adhesive and resistant surfaces based on chitosan/polystyrene sulfonate (CHI/PSS) multilayer membranes is presented. Adsorption behavior of bovine serum albumin (BSA) and lysozyme to CHI/PSS multilayer was studied by simple adsorption method and under pressure driven (ultrafiltration) conditions. The protein incorporated membranes were characterized by FT-IR, UV–vis, SEM and AFM. The loading of proteins to the multilayer was found to be dependent on the nature of protein, pH, number of bilayers, methods of adsorption and time of adsorption. Simple adsorption resulted in BSA adhesive layers with some conformational changes at higher number of bilayers. Ultrafiltration leads to protein repellence at higher number of bilayers which is attributed to the presence of irremovable water. Lysozyme adsorption/sorption varied with pH. Surface coverage dominates at pH close to pI and at pH 5 under ultraflitration condition where as simple adsorption resulted in protein repellence at pI. The secondary structure of adsorbed lysozyme is preserved for a wide pH range (5–11). Desorption study of lysozyme adsorbed membranes at pH 8.8 was carried out to understand the adsorption/sorption of protein. Diffusion of the sorbed lysozyme from the inner layers to the surface is found to take place at lower concentrations of NaCl.