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Related Concept Videos

Coronavirus01:29

Coronavirus

Coronaviruses, including the severe acute respiratory syndrome coronavirus (SARS-CoV), are enveloped viruses characterized by their single-stranded, positive-sense RNA genome and helical nucleocapsid structure. The hallmark of these viruses is their club-shaped spike (S) glycoproteins that protrude from the viral envelope, facilitating attachment to host cells. Typically, coronaviruses infect the upper respiratory tract, often causing mild or asymptomatic disease. However, certain strains like...
Antihypertensive Drugs: Angiotensin-Converting Enzyme Inhibitors01:30

Antihypertensive Drugs: Angiotensin-Converting Enzyme Inhibitors

Angiotensin-converting enzyme (ACE), a vital component of the renin-angiotensin-aldosterone system, is abundant in lung endothelial cells. ACE converts the inactive decapeptide, angiotensin I, into the active octapeptide, angiotensin II. This potent vasoconstrictor narrows blood vessels, increasing resistance to blood flow and elevating blood pressure. Angiotensin II also stimulates aldosterone production, encouraging kidney cells to reabsorb more sodium and water from urine, thereby increasing...
Indirect-Acting Cholinergic Agonists: Mechanism of Action01:18

Indirect-Acting Cholinergic Agonists: Mechanism of Action

Indirect-acting cholinergic agonists work by interacting with an enzyme called acetylcholinesterase (AChE) in the synaptic cleft. They can be reversible or irreversible inhibitors and have different effects on the enzyme.
Reversible inhibitors like edrophonium bind to a specific part of the enzyme called the anionic catalytic site. They form noncovalent bonds, which means they are not strongly attached to the enzyme. This creates a temporary and less stable enzyme–inhibitor complex, leading to...
Allosteric Regulation01:08

Allosteric Regulation

Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...
Allosteric Regulation01:08

Allosteric Regulation

Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...
Enzyme Inhibition01:30

Enzyme Inhibition

Inhibitors are molecules that reduce enzyme activity by binding to the enzyme. In a normally functioning cell, enzymes are regulated by a variety of inhibitors. Drugs and other toxins can also inhibit enzymes. Some inhibitors bind to the enzyme’s active site, while others inhibit enzymatic activity by binding to other sites on the protein structure.

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Related Experiment Video

Updated: Jun 24, 2026

Procedures for the Identification of SARS-CoV-2 Entry Inhibitors as Potential Antivirals using MLV-Based Pseudoviruses
11:43

Procedures for the Identification of SARS-CoV-2 Entry Inhibitors as Potential Antivirals using MLV-Based Pseudoviruses

Published on: February 27, 2026

Allosteric Targeting of the ACE2 Dimer Interface by a Medium-sized Compound Inhibits SARS-CoV-2 Entry.

Mariko Yokogawa1, Shunki Kaneichi1, Mahoro Horiuchi1

  • 1Faculty of Pharmacy, Division of Physics for Life Functions, Keio University, Tokyo 105-8512, Japan.

Journal of Molecular Biology
|June 22, 2026
PubMed
Summary

Researchers discovered a new way to inhibit SARS-CoV-2 (the virus that causes COVID-19) by targeting the ACE2 protein. A novel compound binds to ACE2, altering its shape to block viral entry and suppress infection.

Keywords:
ACE2 dimerSARS-CoV-2medium-sized moleculeprotein–protein interactionsolution NMR

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Last Updated: Jun 24, 2026

Procedures for the Identification of SARS-CoV-2 Entry Inhibitors as Potential Antivirals using MLV-Based Pseudoviruses
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Published on: February 27, 2026

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Profiling of Surface Protein Epitopes on Viral Particles by Multiplex Dual-Reporter Strategy
08:07

Profiling of Surface Protein Epitopes on Viral Particles by Multiplex Dual-Reporter Strategy

Published on: January 12, 2024

Area of Science:

  • Biochemistry
  • Virology
  • Drug Discovery

Background:

  • Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) uses the ACE2 receptor for host cell entry.
  • Existing treatments do not directly inhibit the spike protein-ACE2 interaction.

Purpose of the Study:

  • To discover novel inhibitors of SARS-CoV-2 entry by targeting the ACE2 receptor.
  • To identify compounds that disrupt the interaction between the SARS-CoV-2 spike protein and ACE2.

Main Methods:

  • Artificial intelligence-guided virtual screening of medium-sized compounds.
  • Nuclear magnetic resonance (NMR) spectroscopy to determine compound binding.
  • Infection assays and docking simulations using ACE2 mutants.

Main Results:

  • A novel compound was identified that suppresses SARS-CoV-2 infection by binding to ACE2.
  • The compound binds to a region near the ACE2 dimer interface, distinct from the viral binding site.
  • Compound binding appears to stabilize a looser ACE2 dimer conformation, hindering viral entry.

Conclusions:

  • A previously unknown allosteric regulatory site on ACE2 was identified.
  • Medium-sized molecules targeting this site can modulate ACE2 conformation to inhibit SARS-CoV-2 infection.
  • This discovery opens new avenues for developing COVID-19 therapeutics.