Title:Effect of Calebin-A on Critical Genes Related to NAFLD: A
Protein-Protein Interaction Network and Molecular Docking Study
Volume: 25
Issue: 2
Author(s): Ali Mahmoudi, Mohammad Mahdi Hajihasani, Muhammed Majeed, Tannaz Jamialahmadi and Amirhossein Sahebkar*
Affiliation:
- Department of Medical Biotechnology, Biotechnology Research Center, Pharmaceutical Technology Institute, Mashhad University of Medical Sciences, Mashhad, Iran
- Applied Biomedical Research Center, Mashhad University of Medical Sciences,
Mashhad, Iran
Keywords:
Calebin-A , functional enrichment analysis, GEO, molecular docking, NAFLD, prediction databases, PPI network.
Abstract:
Background: Calebin-A is a minor phytoconstituent of turmeric known for its activity
against inflammation, oxidative stress, cancerous, and metabolic disorders like Non-alcoholic fatty liver disease(NAFLD). Based on bioinformatic tools. Subsequently, the details of the interaction of critical proteins with Calebin-A were investigated using the molecular docking technique.
Methods: We first probed the intersection of genes/ proteins between NAFLD and Calebin-A
through online databases. Besides, we performed an enrichment analysis using the ClueGO plugin
to investigate signaling pathways and gene ontology. Next, we evaluate the possible interaction of
Calebin-A with significant hub proteins involved in NAFLD through a molecular docking study.
Results: We identified 87 intersection genes Calebin-A targets associated with NAFLD. PPI network analysis introduced 10 hub genes (TP53, TNF, STAT3, HSP90AA1, PTGS2, HDAC6,
ABCB1, CCT2, NR1I2, and GUSB). In KEGG enrichment, most were associated with Sphingolipid, vascular endothelial growth factor A (VEGFA), C-type lectin receptor, and mitogen-activated protein kinase (MAPK) signaling pathways. The biological processes described in 87 intersection genes are mostly concerned with regulating the apoptotic process, cytokine production,
and intracellular signal transduction. Molecular docking results also directed that Calebin-A had a
high affinity to bind hub proteins linked to NAFLD.
Conclusion: Here, we showed that Calebin-A, through its effect on several critical genes/ proteins
and pathways, might repress the progression of NAFLD.