Phylogenetic and In Silico Analysis of Interferon Beta-1b Protein

Background and 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.
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.
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).
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.