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We study drag reduction of a uniform flow over a flat surface due to a series of rectangular microgrooves created on the surface. The results reveal that making grooves on the surface usually leads to the generation of secondary vortices inside the grooves that, in turn, decreases the friction drag force and increases the pressure drag force. By increasing the thickness of the grooves to the thickness of the obstacle, the pressure drag increases due to the enhancement of the generated vortices and the occurrence of separation phenomenon and the friction drag reduces due to a decrease of the velocity gradient on the surface. In addition, by increasing the grooves depth ratio, the pressure drag coefficient decreases and the friction drag coefficient increases. However, the impact of the pressure drag coefficient is higher than that of the friction drag coefficient. From a specific point, increasing the groove depth ratio does not effect on decreasing the total pressure drag of the plate. Therefore, creating the grooves in flat surfaces would reduce the total drag coefficient of the plate if the thickness of the grooves does not exceed a specific size and the depth of the grooves is chosen to be sufficiently large. The lattice-Boltzmann method (LBM) is used and the optimal reduction of the drag coefficient is calculated. It is found that for the width ratio equal to 0.19 and the groove depth ratio equal to 0.2548, about 7% decrease is achieved for the average total drag.

Interest in the design and manufacture of RNA and DNA aptamers as apta-biosensors for the early diagnosis of blood infections and other inflammatory conditions has increased considerably in recent years. The practical utility of these aptamers depends on the detailed knowledge about the putative interactions with their target proteins. Therefore, understanding the aptamer-protein interactions at the atomic scale can offer significant insights into the optimal apta-biosensor design. In this study, we consider one RNA and one DNA aptamer that were previously used as apta-biosensors for detecting the infection biomarker protein TNF-α, as an example of a novel computational workflow for selecting the aptamer candidate with the highest binding strength to a target. We combine information from the binding free energy calculations, molecular docking, and molecular dynamics simulations to investigate the interactions of both aptamers with TNF-α. The results reveal that the RNA aptamer has a more stable structure relative to the DNA aptamer. Interaction of aptamers with TNF-α does not have any negative effect on its structure. The results of molecular docking and molecular dynamics simulations suggest that the RNA aptamer has a stronger interaction with the protein. Also, these findings illustrate that basic residues of TNF-α establish more atomic contacts with the aptamers compared to acidic or pH-neutral ones. Furthermore, binding energy calculations show that the interaction of the RNA aptamer with TNF-α is thermodynamically more favorable. In total, the findings of this study indicate that the RNA aptamer is a more suitable candidate for using as an apta-biosensor of TNF-α and, therefore, of greater potential use for the diagnosis of blood infections. Also, this study provides more information about aptamer-protein interactions and increases our understanding of this phenomenon.