| Autor: |
Rangra, Sabita, Chakraborty, Rajkumar, Hasija, Yasha, Aggarwal, Kamal Krishan |
| Zdroj: |
Journal of Biomolecular Structure and Dynamics; December 2023, Vol. 41 Issue: 20 p10985-10998, 14p |
| Abstrakt: |
AbstractRheumatoid arthritis (RA) is an auto-immune disease that affects the synovial lining of the joints, causes synovitis and culminates to joint destruction. Cathepsin B is responsible for digesting unwanted proteins in extracellular matrix but its hyper expression could implicate in pathological diseases like RA. Available treatments for RA are classified into non-steroidal anti-inflammatory drugs (NSAIDs), disease-modifying anti-rheumatic drugs (DMARDs), and steroids, but the severe side effects associated with these drugs is one of concerns and cannot be ignored. Thus, any alternative therapy with minimum or no side effects would be a cornerstone. In our in silicostudies a cystatin C similar protein (CCSP) has been identified from Musa acuminatathat could effectively inhibit the cathepsin B activity. In silicoand molecular dynamics studies showed that the identified CCSP and cathepsin B complex has binding energy −66.89 kcal/mol as compared to cystatin C - cathepsin B complex with binding energy of −23.38 kcal/mol. These results indicate that CCSP from Musa acuminatahas better affinity towards cathepsin B as compared to its natural inhibitor cystatin C. Hence, CCSP may be suggested as an alternative therapeutic in combating RA by inhibiting its one of the key proteases cathepsin B. Further, in vitroexperiments with fractionated protein extracts from Musasp. peel inhibited cathepsin B to 98.30% at 300 µg protein concentration and its IC50was found to be 45.92 µg indicating the presence of cathepsin B inhibitor(s) in protein extract of peel which was further confirmed by reverse zymography.Communicated by Ramaswamy H. Sarma |
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