PMID- 37274904
OWN - NLM
STAT- MEDLINE
DCOM- 20230613
LR  - 20230613
IS  - 2008-9872 (Electronic)
IS  - 0365-3439 (Print)
IS  - 0365-3439 (Linking)
VI  - 77
IP  - 6
DP  - 2022 Dec
TI  - 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.
PG  - 2181-2186
LID - 10.22092/ARI.2022.358070.2145 [doi]
AB  - 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 A. 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.
FAU - Danaeifar, M
AU  - Danaeifar M
AD  - Department of Medical Biotechnology, School of Advanced Technologies in Medicine, 
      Tehran University of Medical Sciences, Tehran, Iran.
LA  - eng
PT  - Journal Article
DEP - 20221231
PL  - Iran
TA  - Arch Razi Inst
JT  - Archives of Razi Institute
JID - 101549567
RN  - 0 (Blood Glucose)
RN  - 0 (RNA, Viral)
SB  - IM
MH  - Humans
MH  - Blood Glucose
MH  - *COVID-19/veterinary
MH  - *Diabetes Mellitus, Type 2/drug therapy
MH  - Molecular Docking Simulation
MH  - RNA, Viral/therapeutic use
MH  - SARS-CoV-2
PMC - PMC10237550
OTO - NOTNLM
OT  - SARS-CoV-2
OT  - diabetes mellitus
OT  - nsp10
OT  - protein docking
COIS- The author declares that there is no potential conflict of interest related to 
      this research and publication. I hereby confirm that I have reviewed and complied 
      with the relevant Instructions to Authors, the Ethics in Publishing policy, and 
      Conflicts of Interest disclosure.
EDAT- 2023/06/05 19:10
MHDA- 2023/06/07 06:42
PMCR- 2022/12/31
CRDT- 2023/06/05 12:09
PHST- 2022/03/08 00:00 [received]
PHST- 2022/04/07 00:00 [accepted]
PHST- 2023/06/07 06:42 [medline]
PHST- 2023/06/05 19:10 [pubmed]
PHST- 2023/06/05 12:09 [entrez]
PHST- 2022/12/31 00:00 [pmc-release]
AID - ARI-77-6 [pii]
AID - 10.22092/ARI.2022.358070.2145 [doi]
PST - epublish
SO  - Arch Razi Inst. 2022 Dec 31;77(6):2181-2186. doi: 10.22092/ARI.2022.358070.2145. 
      eCollection 2022 Dec.