期刊
ADVANCED PHARMACEUTICAL BULLETIN
卷 9, 期 4, 页码 640-648出版社
TABRIZ UNIV MEDICAL SCIENCES & HEALTH SERVICES
DOI: 10.15171/apb.2019.074
关键词
Interferon Beta; Molecular Docking; Insilico; IFNAR; mHulFN-beta-27-101
资金
- [92042856]
Purpose: Interferon beta (IFN-beta) is used to combat multiple sclerosis (MS) disease. Creating R27T and V101F mutations (mHulFN-beta-27 and mHulFN-beta-101) is one of the tasks performed to improve human interferon beta (HulFN-beta) half-life, function and expression. In this work, the impact of R27T and V101F mutations in recombinant IFN-beta on its binding to interferon receptors were studied by molecular docking. Methods: This work was performed through in silica study. The simulation of mutation was performed using the online Rosetta Backrub software and checked using server verify3D. Comparison of access to the solvent of the amino acids in the structures created was performed using the asaview online server. Also, the effect of mutations on the fold of the protein was reviewed by the online HOPE server. The molecular docking was performed between HulFN-beta and the external region of IFNAR receptor using the online ClusPro2 protein-protein docking server. Results: The comparison of the values of the negative binding energy (Delta Gbind) obtained from protein-protein molecular docking between IFNAR receptor and HulFN-beta, mHulFN-beta-27, mHulFN-beta-101 and mHulFN-beta-27-101 ligands did not show a significant difference, and these differences do not see any meaningful relationship between them (P > 0.9999). Conclusion: Regarding these results, it can be concluded that these mutations do not have a negative effect on the composition of the complex rHulFN-beta/IFNAR. So, they do not interfere with the binding of the IFN-beta to the receptor. It is concluded that the quality of the rHulFN-beta is improved by introducing these two mutations.
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