Abstract
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•First theoretical study focused on Renin Receptor against Renin for Hypertension management.•SBVS performed to identify the potent inhibitor for Renin Receptor.•Enamine_48562 and Maybridge_24657 are highly effective in binding maltose-free structures.•Enamine_95473 and Maybridge_33378 compounds are potent in binding maltose-bound structures.
The structural finding of the receptor for prorenin/renin (PRR) has brought new insights into the structural and physiological role of the renin-angiotensin-aldosterone system (RAAS). The constant process of exploring all other possibilities in research could lead to alternative and attractive discoveries. This study was employed with maltose-free and maltose-bound crystal structures of Renin Receptor with intra-cellular domain region. We have identified two lead compounds, Enamine_48562 and Maybridge_24657, that are highly effective in binding maltose-free structures, while Enamine_95473 and Maybridge_33378 are the most potent in binding maltose bound structures. The binding energy profile demonstrates the lead compounds' high binding affinity. Molecular dynamics simulation studies were also used to investigate the stability and conformational changes. Meanwhile, significant experimental investigations are needed to support theoretical findings.