A Non-Structural Protein of Severe Acute Respiratory Syndrome Coronavirus 2 with a Potential Ability to Reduce Blood Glucose for Use in Controlling Type 2 Diabetes Mellitus

• Published in: Archives of Razi Institute Vol. 77; no. 6; pp. 2181 - 2186
• Main Author: Danaeifar, M
• Format: Journal Article
• Language: English
• Published: Iran Razi Vaccine & Serum Research Institute 01.12.2022
• Subjects: Blood Glucose; COVID-19 - veterinary; Diabetes Mellitus, Type 2 - drug therapy; Diabetes Mellitus, Type 2 - veterinary; Humans; Molecular Docking Simulation; Original; RNA, Viral - therapeutic use; SARS-CoV-2; SARS-CoV-2; diabetes mellitus; protein docking; nsp10
• ISSN: 0365-3439; 2008-9872
• DOI: 10.22092/ARI.2022.358070.2145

It is estimated that more than 400 million people worldwide are suffering from diabetes. There are two types of diabetes. Type 1 diabetes is the result of insufficient insulin secretion into the bloodstream, most often due to an autoimmune attack on the pancreas glands. Type 2 diabetes is caused by the inability of the surface ligands to adsorb the insulin from the bloodstream. The conventional medicines for diabetes mellitus include sulfonylureas, biguanide, thiazolidinediones, alpha-glucosidase inhibitors, and meglitinide. By February 2022, Severe acute respiratory syndrome coronavirus 2 (SARSCoV2) had infected more than 391 million people worldwide, claiming 5.7 million lives and imposing heavy costs on the healthcare system. The present study aimed to assess the potential use of this non-structural SARS-CoV-2 protein in the treatment of type 2 diabetes mellitus. The nsp10 was structurally aligned with GoDrugBank therapeutic agents, and lixisenatide was found to have the most similar chemical structure. This drug is a glucagon-like peptide-1 (GLP1) receptor agonist used for the treatment of type 2 diabetes mellitus. The best molecular docking energy score for these two proteins was -301.47, and the ligand root mean square deviation was calculated to be 107.93 Å. The molecular dynamics for the stability of the nsp10 and GLP1R binding in triplicate for 150 ns demonstrated that the nsp10-GLP1R remained bound for more than 80 ns. This study indicated that the nsp10 protein can be further studied to be used as an antidiabetic medication.