Protein-polyelectrolyte complexes (PPC) are playing an important role in a variety of chemical and biological processes, such as protein separation, enzyme stabilization, and polymer drug delivery. The present investigation is focused on evaluation of the PPC formation between a synthetic polypeptide (poly(aspartic acid) -PAS) and a natural protein (bovine serum albumin -BSA). The PPC obtained from PAS and BSA in different ratio was investigated by corroboration of various techniques of characterization as: spectroscopy, microscopy, thermogravimetric analysis, dynamic light scattering (DLS), and zeta potential determination, measurements which were performed in static and/or dynamic conditions. The static contact angle of the sample films was also determined in order to evaluate the changes brought upon surface free energy of the prepared PPCs in interdependence with the complexes composition. The critical conditions for complex formation in BSA-polyelectrolyte systems were underlined. The phenomenon was better evidenced in case of a ratio of 1/1 wt between the two polymers, both in static and/or dynamic conditions.