Myelin basic protein (MBP) is one of the main protein components of central nervous system that as shown in our work, under appropriate condition, forms spherulites. The structural and morphological features of these elements and the ability of trehalose to decrease or completely avoid their formation have been clarified with different but complementary techniques. The FTIR spectra provided compelling evidence for the presence of a small amount of elements organized in secondary structures such as helices and sheets. Polarized optical microscope observations show the presence of spherulites with an average size ranged from 41 to 61 μm, characterized by non-birifrangent core. The fluorescence data supply useful informations that are consistent with the presence of a molecular exclusion effect, following interaction of the disaccharide with protein that involves the environment around the single tryptophan residue. Moreover, study of protein conformational states by SDS-PAGE, let us to state that trehalose completely avoid autocatalytic cleavage properties of MBP up to 4 days of incubation at 37 °C and pH 7.4.