Exploring the Potential of Calebin-A in Targeting Obesity-Related Genes and Pathways
Journal of Cellular and Molecular Medicine, cilt.30, sa.11, 2026 (SCI-Expanded, Scopus)
- Yayın Türü: Makale / Tam Makale
- Cilt numarası: 30 Sayı: 11
- Basım Tarihi: 2026
- Doi Numarası: 10.1111/jcmm.71244
- Dergi Adı: Journal of Cellular and Molecular Medicine
- Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, BIOSIS, EMBASE, MEDLINE, Directory of Open Access Journals, Natural Science Collection (ProQuest), Biological Science Database (ProQuest), Biomedical Reference Collection: Corporate Edition (EBSCO), Health Research Premium Collection (ProQuest), Pharma Collection (ProQuest)
- Anahtar Kelimeler: bioinformatics, calebin-A, gene expression, molecular docking, obesity, pathway analysis
- Çanakkale Onsekiz Mart Üniversitesi Adresli: Evet
Özet
Obesity is a global health crisis affecting millions, associated with metabolic disorders such as type 2 diabetes and cardiovascular disease. Calebin-A, a bioactive compound derived from Curcuma species, has shown promise in managing obesity and its complications. This study utilized bioinformatics tools to explore the molecular mechanisms of Calebin-A in obesity. Transcriptomic data from obese and normal omental adipose tissue (GSE286454) were analysed, identifying 317 differentially expressed genes (DEGs). Functional enrichment analysis indicated a notable engagement of lysosomal activity, immune response, cell migration, axon guidance and apoptosis pathways. A STRING-based protein–protein interaction network revealed nine hub genes through a composite centrality score. Among these, CTSB, CTSZ, CTSA, GRN and TUBB exhibited upregulation and were prioritized for subsequent analysis. External validation (GSE59034; 16 obese vs. 16 controls) corroborated the consistent upregulation of CTSB, CTSZ, GRN and CTSA. Target prediction analysis identified 443 potential targets for Calebin-A, with pathway-level overlap suggesting a convergence on immune, lysosomal and cytoskeletal processes. Molecular docking studies indicated favourable binding affinities (−5.2 to −7.1 kcal/mol), with CTSZ demonstrating the most robust interaction. A 100 ns molecular dynamics simulation validated structural stability and indicated favourable binding free energy (MM-PBSA ΔG ≈ −110 kJ/mol). Results suggest that Calebin-A targets genes and proteins involved in energy balance and inflammation, offering insights into its anti-obesity potential. These findings provide a foundation for experimental validation and therapeutic development.