Recombinant human interferon α-2b (rhIFNα-2b) is a widely used therapeutic protein for the treatment of viral infections such as hepatitis. Being a therapeutic protein it is only active in its native conformation so that it is important to investigate possible pathways of degradation when producing it. In this work rhIFNα-2b was subjected to four different stress conditions and the resulting products characterized with fluorescence spectroscopy, fluorescence anisotropy, circular dichroism, dynamic light scattering and scanning electron microscopy. The results showed that rhIFNα-2b loses its native conformation in all conditions in which it was tested and there was formation of aggregates. It was also made a bioactivity assay where we saw that the protein had biological activity before and after the stress conditions
