Abstract:
A microstructural analysis of the human serum albumin (HSA) samples dehydrated on a glass substrate from solutions with different concentrations of protein has been performed. The structuring effect of salt (NaCl) on the variations in the morphology of HSA interfaces has been shown experimentally. The substantiation of some structural effects has been given by taking into consideration the supramolecular organization and the polyelectrolyte nature of the protein molecule.