The inter-base pair interactions (hydrogen bonds) were initially computed from the aptamer sequence using the Vfold2D software. In the next step, these structures were converted to 3D structures using Vfold3D; the 2D picture was displayed in Figure , and Table presented the dot-bracket notation. These 3D structures were then used for molecular docking simulations to obtain protein-aptamer complexes. The protein-aptamer interactions were computed using the PLIP webserver. Based on PLIP analysis, the NC4 aptamer binds to the TNF-α by forming 17 hydrogen bonds and one salt bridge. On the other hand, the TNF aptamer interacts with the TNFα by making 17 hydrogen bonds and 4 salt bridges. The NT-proBNP aptamer binds to the TNF-α by forming 19 hydrogen bonds and 4 salt bridges. The TNF-α M1, on the other hand, has 16 hydrogen bonds and 2 salt bridges while the TNF-α M2 also has 2 salt bridges but21 hydrogen bonds. TNF-α M3 has 25 hydrogen bonds with no salt bridges, and the M4 TNF-α mutation has 4 21 hydrogen bonds with 3 salt bridges. Finally, protein-aptamer binding energy was computed using a PDA-pred webserver to obtain the strength of interactions. Which shows that To understand the structure and size of the TNF-alpha and TACE enzymes, we have predicted their complete 3D structure in Figure . This structure depicts that the TNF-alpha has three regions: (a) soluble head region, (b) middle transmembrane region, and (c) bottom cytoplasmic region. Based on these structures, we propose that for the cleavage, TNF-alpha first moves up so the stem region is exposed and reaches the same height as the TACE enzyme. Once the enzyme reaches too the stem region, it cleaves, resulting in the release of the TNF-alpha subunit.