Statins and COVID-19 (Mechanism of Action, Effect on Prognosis)

Lewek, Joanna; Surma, Stanisław; Banach, Maciej

doi:10.1007/978-3-031-15478-2_17

Cited by 2 publications

(1 citation statement)

References 76 publications

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“…However, it is worth noting that elevated blood cholesterol levels could potentially heighten the risk of heart-related illnesses [ 6 , 7 , 8 ]. Statins stand out among the extensively researched cholesterol derivatives [ 3 , 9 ], given their remarkable efficacy in lowering cholesterol levels in individuals with hypercholesterolemia [ 10 , 11 ] as well as their application in various other treatments [ 12 ]. The mechanism of action of statins involves the inhibition of HMG-CoA reductase [ 10 ], an enzyme responsible for cholesterol synthesis in the liver.…”

Section: Introductionmentioning

confidence: 99%

Exploration of Binding Affinities of a 3β,6β-Diacetoxy-5α-cholestan-5-ol with Human Serum Albumin: Insights from Synthesis, Characterization, Crystal Structure, Antioxidant and Molecular Docking

Alam

2023

Molecules

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The present study describes the synthesis, characterization, and in vitro molecular interactions of a steroid 3β,6β-diacetoxy-5α-cholestan-5-ol. Through conventional and solid-state methods, a cholestane derivative was successfully synthesized, and a variety of analytical techniques were employed to confirm its identity, including high-resolution mass spectrometry (HRMS), Fourier transforms infrared (FT-IR), nuclear magnetic resonance (NMR), elemental analysis, and X-ray single-crystal diffraction. Optimizing the geometry of the steroid was undertaken using density functional theory (DFT), and the results showed great concordance with the data from the experiments. Fluorescence spectral methods and ultraviolet–vis absorption titration were employed to study the in vitro molecular interaction of the steroid regarding human serum albumin (HSA). The Stern-Volmer, modified Stern-Volmer, and thermodynamic parameters’ findings showed that steroids had a significant binding affinity to HSA and were further investigated by molecular docking studies to understand the participation of active amino acids in forming non-bonding interactions with steroids. Fluorescence studies have shown that compound 3 interacts with human serum albumin (HSA) through a static quenching mechanism. The binding affinity of compound 3 for HSA was found to be 3.18 × 104 mol−1, and the Gibbs free energy change (ΔG) for the binding reaction was −9.86 kcal mol−1 at 298 K. This indicates that the binding of compound 3 to HSA is thermodynamically favorable. The thermodynamic parameters as well as the binding score obtained from molecular docking at various Sudlow’s sites was −8.2, −8.5, and −8.6 kcal/mol for Sites I, II, and III, respectively, supporting the system’s spontaneity. Aside from its structural properties, the steroid demonstrated noteworthy antioxidant activity, as evidenced by its IC50 value of 58.5 μM, which is comparable to that of ascorbic acid. The findings presented here contribute to a better understanding of the pharmacodynamics of steroids.

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