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The pathological hallmark of Alzheimer's disease is the accumulation of peptides in human brains. These peptides can be degraded by several enzymes such as hACE, hECE, hIDE and cathepsin B. Out of which cathepsin B also belongs to the papain super family and has been found in human brains, it has a role in peptide degradation through limited proteolysis. The concentrations are maintained properly by its production and clearance via receptor-mediated cellular uptake and direct enzymatic degradation. However, the reduced production of degrading enzymes as well as their degrading activity in human brains initiate the process of accumulation of peptides. So it becomes essential to investigate the molecular interactions involved in the process of degradation in detail at the atomic level. Hence, homology modeling, molecular docking and molecular dynamics simulation techniques have been used to explore the possible role of cathepsin B from Hordeum vulgare in the degradation of amyloid beta (Aβ) peptides. The homology model of cathepsin B from Hordeum vulgare shows good similarity with human cathepsin B. Molecular docking and MD simulation results revealed that the active site residues Cys32, HIS112, HIS113 are involved in the catalytic activity of cathepsin B. The sulfhydryl group of the Cys32 residue of cathepsin B from Hordeum vulgare cleaves the peptide from the carboxylic end of Glu11. Hence, this structural study might be helpful in designing alternative strategies for the treatment of AD.


Maruti J Dhanavade, Rishikesh S Parulekar, Subodh A Kamble, Kailas D Sonawane. Molecular modeling approach to explore the role of cathepsin B from Hordeum vulgare in the degradation of Aβ peptides. Molecular bioSystems. 2016 Jan;12(1):162-8

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PMID: 26568474

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