In silico binding affinity predictions of potential angiotensin-I converting enzyme (ACE) inhibitor kaempferol glycosides

We sought to understand the efficacy of the small molecule kaempferol glycosides as an angiotensin I-converting enzyme (ACE) inhibitor. ACE is important in mediating the Renin-Angiotensin-Alodosterone System (RASS) and blood pressure in humans. Previous research has elucidated the potential ability of small-molecules to serve as effective ACE inhibitors. This present study, and data, therefore, shed light on the kaempferol glycoside’s ability to effectively bind to the ACE receptor. 3D structures and STL files of common ACE inhibitors were derived from PubChem and relevant data was obtained from the RCSB Protein Data Bank. Molecular docking analysis was conducted using UCSF Chimera and iGemDock software. Specific binding sites, i.e. residues, were determined through the 3DLigandSite virtual tools. The data demonstrate the ability of kaempferol glycosides to antagonistically compete, and even outperform, some marketed ACE inhibitors. Data such as h-bonding and the energy released may be interpreted to represent the magnitude of the thermodynamic mediation of the specific receptor-ligand binding complex. Greater energy released is generally indicative of a more effective binding. Future research should use in-silico methods and computational chemistry in order to assist in the discovery of small-molecule targets for ACE-inhibition