Key result
Val-Trp dipeptide demonstrates strong in silico binding affinity and stability with ACE.
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Hypertension is a significant risk factor for various diseases, especially heart, brain, and kidney diseases. It is known that many peptides have the property of lowering blood pressure and determine as ACE inhibitors. The purpose of this study is to obtain information about the molecular structure of Val-Trp (L-valyl-L-tryptophan), which is one of the antihypertensive peptides, by molecular mechanical, quantum mechanical, and spectroscopic methods (FT-IR and Raman). Also, it is aimed to investigate the interactions of Val-Trp dipeptide with receptors related to hypertension and to determine the pharmacokinetic profile due to the potential of the peptide to be a drug candidate. The peptide structure was optimized by DFT/B3LYP/6-311++G(d,p) basis set, then vibrational wavenumbers, molecular electrostatic potential (MEP), HOMO-LUMO (highest occupied molecular orbital- lowest unoccupied molecular orbital), NBO (natural bond orbital) analyzes were performed. The assignment of fundamental theoretical vibration wavenumbers was carried out with potential energy distribution analysis (PED). After the structural analyzes of the peptide were performed, the interactions of the peptide with Angiotensin-converting enzyme (ACE), Angiotensin II Receptor Type 1 (AT1R) and Renin were investigated by molecular docking study. Then, the molecular dynamic (MD) simulation of the peptide-ACE complex with the best binding affinity in the molecular docking studies was carried out for 50 ns. ADME (absorption, distribution, metabolism, and excretion) analysis of Val-Trp dipeptide was performed. In support of the studies carried out, enlightening information about the feasibility of the antihypertensive drug of Val-Trp dipeptide with the help of the ADME profile was presented to the literature.Communicated by Ramaswamy H. Sarma.
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Bilge Bıçak (2023) studied Hypertension. Val-Trp (L-valyl-L-tryptophan) dipeptide was evaluated on Interactions with ACE, AT1R, and Renin via molecular docking, 50 ns molecular dynamics simulation, and ADME pharmacokinetic profile. Val-Trp dipeptide showed its best molecular docking binding affinity with angiotensin-converting enzyme (ACE), which was further evaluated in a 50 ns molecular dynamics simulation and ADME analysis.
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