Background and purpose: Interferon beta-1b recombinant protein is used for reducing the relapse rate and treatment in patients with Multiple sclerosis (MS). In this study, phylogenetic and in silico analysis of interferon beta-1b were conducted by servers and bioinformatics tools to predict its structural potential.

Materials and methods: Physiological and physico-chemical characteristics of interferon beta-1b protein were evaluated by ProtScale and ProtParam servers, respectively. The 3D structure of the interferon beta-1b protein and its interaction with other proteins were studied using Swiss-Model server and the STRING platform, respectively.

Results: The results of the phylogenetic analysis showed that the human interferon beta protein is closest to Daubenton's bat in the amino acid structure by 96%. The in silico analysis of interferon beta 1b protein implied the existence of signal peptide and lack of the transmembrane domain. The results of post-translational modification predictions showed that protein acetylation and phosphorylation may occur in some regions of interferon beta-1b protein. The analysis of the protein networking of interferon beta-1b revealed more interactions between this protein and interferon receptor 1 (IFNAR1) and interferon regulatory factor 3 (IRF3).

Conclusion: In Silico analysis showed that interferon beta-1b, is a protein with effective regulatory role but unstable in vitro. This bioinformatic analysis of interferon beta-1b protein can provide the groundwork for practical tests and future functional studies.