Introduction:

breast cancer has increased by 50% in the last two decades. Cathepsin B is a protease involved in the process of tumorigenesis. One of the current problems is the emergence of drug resistance. The search for new therapeutic alternatives can reduce its morbidity and mortality.

Objective:

in-silico structural and functional characterization of the conserved region in Cathepsin B as a potential therapeutic target in the treatment of breast cancer.

Methods:

using the NCBI ENTREZ tool 2,485 Cathepsin B sequences were obtained. The sequences were subjected to multiple alignments using Clustall Omega 1.2.4. Structural and functional characterization of the protease under study was performed using the InterPro, Prosite, Uniprot and UniprotKB databases. Using the Jalview viewer, the largest conserved area of Cathepsin B species was chosen.

Results:

the protease is involved in the regulation of catalytic activity, proteolysis, negative regulation of cell death, collagen catabolic processes and possesses hydrolase activity. The multiple analyses allowed the visualization of the aminoacid characteristics of the active site of Cathepsin B and the selection of the most conserved protein region.

Conclusions:

the conserved region of Cathepsin B constitutes a potential target in the development of inhibitors as drugs against breast cancer. In-silico analysis reduces the cost of current research and contributes to pharmacological biosafety.

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