AN FTIR STUDY OF THE STRUCTURE OF HUMAN SERUM-ALBUMIN ADSORBED TO POLYSULFONE

Internal reflection infrared spectroscopy was employed in a study of t he structural changes in human serum albumin that result from adsorpti on to cast films of polysulfone. Adsorption experiments were carried o ut in a flow-through cell at 30 degrees C in the presence of either a H2O-based or D2O-based saline buffer. Spectral features show adsorptio n results in Amide I bandwidth broadening and diminished Amide II band intensities relative to the Amide I band. Deconvolution and band-fitt ing of spectra obtained in the presence of D2O show appearance of beta and aperiodic conformations at the expense of helical structures. The results suggest considerable change in the secondary structure of hum an serum albumin upon adsorption to polysulfone.