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Luteolin could be used to inhibit COVID-19 virus, research finds

In the race to find potential treatments for SARS-CoV-2, the virus that causes COVID-19, researchers have often focused on how to disrupt the functional proteins on the virus’s active binding site — the spike that binds to human cells.

Juan de Pablo
Prof. Juan de Pablo

But using simulations, researchers at the Pritzker School of Molecular Engineering (PME) at the University of Chicago have found a different way to disrupt the virus: through compounds that bind at a previously unidentified distant binding site (far from the main active site) of one of the virus’ proteins, thereby destabilizing it and inhibiting its ability to replicate.

They also found that an existing natural compound, luteolin, interacts in this way with the SARS-CoV-2 virus.

“Understanding this mechanism could pave the way for future drug discovery,” said Prof. Juan de Pablo, who led the research. The results were published in the journal Molecular Systems and Design Engineering.

Using computer simulations to understand potential treatments

Since the beginning of the pandemic, de Pablo and his group have been using advanced computational simulations to systematically look at the different proteins that allow the virus to replicate or infect cells. They also have looked at key drugs that are already used to treat other diseases and could be repurposed to inhibit those processes in SARS-CoV-2. The simulations, which require months of extremely powerful computations, ultimately reveal what happens to the virus at the molecular level.

Previously, the group used computational analysis to reveal how the drug Ebselen binds to the virus’s main protease, or MPro. In a different study, they also revealed how the antiviral drug remdesivir binds to and interferes with the virus.

In this new research, they used molecular simulations to decipher how compounds bind to the virus and lead to an allosteric effect, which means they produce changes throughout the virus, not just at the binding site. These changes propagate throughout the protein and inhibit its ability to form complexes with other proteins, making the virus less efficient and hindering its ability to replicate.

“Many studies look at how well drugs fit within the active site of the protein, but we are looking at all the places where drugs could possibly bind,” de Pablo said. “Because we examined in detail all such sites, we found this new allosteric mechanism and a potential new way to interfere with the disease.”

Accelerating discoveries for new treatments

The researchers found that a natural compound, luteolin, binds to the virus in this manner – information that could help lead to new treatments for the virus. More specifically, they demonstrated that luteolin alters the protein-protein complex that is formed between the receptor binding domain (RBD) of SARS-CoV-2 and the angiotensin-converting enzyme 2 (ACE2), which is crucial for viral entry and subsequent replication.

The group is continuing to examine the mechanisms of different sets of drugs on different proteins, with the goal of creating a complete landscape of molecular targets.

“We are getting better and faster at systematically finding drugs to treat this virus,” de Pablo said. “We are accelerating discoveries, and we are not too far from finding drugs that will be new, different, and effective. That’s going to be extremely important as this virus continues to mutate and evolve.”

Other authors on the paper include Walter Alvarado, Gustavo R. Perez-Lemus, Cintia A. Menéndez, Fabian Byléhn.

Citation: “Molecular characterization of COVID-19 therapeutics: luteolin as an allosteric modulator of the spike protein of SARS-CoV-2,” Alvarado et. al, September 15, 2021, Molecular Systems and Design Engineering. DOI: doi.org/10.1039/D1ME00119A

Funding: National Science Foundation, Department of Defense, University of Chicago