Effect of divalent ions on the optical emission behavior of protein thin films
Photoluminescence behaviors of proteinthin film, bovine serum albumin (BSA) have been studied in the presence of three divalent ions (Mg{sup 2+}, Ca{sup 2+} and Ba{sup 2+}) at different temperatures using fluorescence spectroscopy. Film thickness and morphology have been studied using atomic force microscopy. Variation of different physicochemical parameters like temperature, solvent polarity, pH, ionic strength, substrate binding etc. can make conformational changes in the protein structure and hence influences the emission behavior.In thin film conformation of BSA, dynamic quenching behavior has beenidentified in the presence of all the three divalent ions at pH≈ 5.5. Depending upon the charge density of the divalent ions interaction with protein molecules modifies and as a result quenching efficiency varies. Also after heat treatment, conformation of the protein molecules changes and as a result the quenching efficiency enhances than that of the unheated films. Studies on such protein-ion interactions and conformational variation may explore various functions of protein when it will adsorb on soft surfaces like membranes, vesicles, etc.