Biologists find dark chocolate may block COVID-19 It is a bold statement so, let's geek out with some science….
Plant Biologists at North Carolina State University have shown the chemical compounds in certain foods, including cacao powder and dark chocolate may interfere with the SARS-CoV-2 virus’ ability to replicate and cause COVID-19 symptoms. BRING ON THE DARK CHOCOLATE!
Honestly, do you need anymore facts to eat dark chocolate? If so, read on!
The Scientists used computer simulations and lab studies to evaluate the potential impact of specific foods and medicinal plants. They researched cacao powder, dark chocolate, muscadine grapes and green tea for their known anti-inflammatory and antioxidant properties.
De-Yu Xie, PhD, professor of plant and microbial biology says proteases (an enzyme that breaks down protein, and peptides) are important to the health and viability of cells and viruses. If proteases are inhibited, cells cannot perform many important functions – like replication, for example. “One of our lab’s focuses is to find nutraceuticals in food or medicinal plants that inhibit either how a virus attaches to human cells or the propagation of a virus in human cells,” Xie said. The simulations showed the compounds in the medicinal foods bound to different portions of the Mpro protein (the so-called “main protease” in the SARS-CoV-2 virus) and filled the “pockets” on the enzyme, disabling its normal functions.
So in easier words to understand, the health benefits in certain foods, including dark chocolate, can inhibit the growth of the virus.
The vitro lab phase of the study found the green tea and grape extracts completely inhibited the Mpro activity and the cacao and dark chocolate reduced the Mpro activity by 40-50%.
“Mpro in SARS-CoV-2 is required for the virus to replicate and assemble itself,” Xie said. “If we can inhibit or deactivate this protease, the virus will die.”
“You get some chocolate! and, you get some chocolate!”
The original research article appears in Frontiers in Plant Science and an abstract of the paper included below.
The research was supported by the U.S. Department of Agriculture.
Docking characterization and in vitro inhibitory activity of flavan-3-ols and dimeric proanthocyanidins against the main protease activity of SARS-Cov-2
Authors: Yue Zhu and De-Yu Xie, NC State University Published: Nov. 30, 2020 in Frontiers in Plant Science DOI: 10.3389/fpls.2020.601316 Department of Plant and Microbial Biology, North Carolina State University, Raleigh, NC, United States Abstract: We report to use the main protease (Mpro ) of SARS-Cov-2 to screen plant flavan-3-ols and proanthocyanidins. Twelve compounds, (–)-afzelechin (AF), (–)-epiafzelechin (EAF), (+)-catechin (CA), (–)-epicatechin (EC), (+)-gallocatechin (GC), (–)-epigallocatechin (EGC), (+)-catechin-3-O-gallate (CAG), (–)-epicatechin-3-O-gallate (ECG), (–)-gallocatechin-3-O-gallate (GCG), (–)-epigallocatechin-3-O-gallate (EGCG), procyanidin A2 (PA2), and procyanidin B2 (PB2), were selected for docking simulation. The resulting data predicted that all 12 metabolites could bind to Mpro . The affinity scores of PA2 and PB2 were predicted to be −9.2, followed by ECG, GCG, EGCG, and CAG, −8.3 to −8.7, and then six flavan-3-ol aglycones, −7.0 to −7.7. Docking characterization predicted that these compounds bound to three or four subsites (S1, S1′, S2, and S4) in the binding pocket of Mpro via different spatial ways and various formation of one to four hydrogen bonds. In vitro analysis with 10 available compounds showed that CAG, ECG, GCG, EGCG, and PB2 inhibited the Mpro activity with an IC50 value, 2.98 ± 0.21, 5.21 ± 0.5, 6.38 ± 0.5, 7.51 ± 0.21, and 75.3 ± 1.29 μM, respectively, while CA, EC, EGC, GC, and PA2 did not have inhibitory activities. To further substantiate the inhibitory activities, extracts prepared from green tea (GT), two muscadine grapes (MG), cacao, and dark chocolate (DC), which are rich in CAG, ECG, GAG, EGCG, or/and PB2, were used for inhibitory assay. The resulting data showed that GT, two MG, cacao, and DC extracts inhibited the Mpro activity with an IC50 value, 2.84 ± 0.25, 29.54 ± 0.41, 29.93 ± 0.83, 153.3 ± 47.3, and 256.39 ± 66.3 μg/ml, respectively. These findings indicate that on the one hand, the structural features of flavan-3-ols are closely associated with the affinity scores; on the other hand, the galloylation and oligomeric types of flavan-3-ols are critical in creating the inhibitory activity against the Mpro activity.