Asset Details
Do you wish to reserve the book?
Pyrogallol B-ring enhances catechin binding to the SARS-CoV-2 spike receptor-binding domain to inhibit interaction with ACE2
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
Pyrogallol B-ring enhances catechin binding to the SARS-CoV-2 spike receptor-binding domain to inhibit interaction with ACE2
Do you wish to request the book?
Pyrogallol B-ring enhances catechin binding to the SARS-CoV-2 spike receptor-binding domain to inhibit interaction with ACE2
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
Pyrogallol B-ring enhances catechin binding to the SARS-CoV-2 spike receptor-binding domain to inhibit interaction with ACE2
2026
Overview
Severe acute respiratory syndrome coronavirus 2 infects host cells through binding of the spike protein receptor-binding domain (RBD) to the human angiotensin-converting enzyme 2 receptor. In this study, the antiviral activity of 14 catechin derivatives was evaluated using a pseudovirus assay that emulates spike-mediated cell fusion. Of these, gallocatechin gallate, epigallocatechin gallate, epigallocatechin 3-(3″-O-methyl) gallate, and epigallocatechin exhibit strong inhibitory effects on infection. A structural comparison of the compounds revealed that catechins with a pyrogallol-type B-ring configuration exhibited greater inhibitory effects than their catechol-type counterparts. Docking simulations demonstrated that the hydroxyl group at the 5-position of the B-ring forms a hydrogen bond with Gln493 on the spike RBD, thereby facilitating additional stabilizing interactions with adjacent residues, such as Tyr453. Although catechin bioavailability is low, the results of this study suggest that regular consumption or gargling may offer localized antiviral activity at mucosal surfaces, such as those found in the oral or nasal cavity, because the catechin concentrations used in the cell assays are similar to those observed in green tea (100 µM). This study underscores the potential of pyrogallol-type catechins to act as antiviral agents.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 631/45
/ ACE2
/ Angiotensin-converting enzyme 2
/ Angiotensin-Converting Enzyme 2 - chemistry
/ Angiotensin-Converting Enzyme 2 - metabolism
/ Animals
/ Antiviral Agents - chemistry
/ Antiviral Agents - pharmacology
/ Betacoronavirus - drug effects
/ Betacoronavirus - metabolism
/ Catechin
/ Catechin - analogs & derivatives
/ Cells
/ Cocoa
/ Enzymes
/ Humanities and Social Sciences
/ Humans
/ Molecular Docking Simulation
/ Nose
/ Protein Binding - drug effects
/ Proteins
/ Science
/ Severe acute respiratory syndrome coronavirus 2
/ Spike Glycoprotein, Coronavirus - chemistry
/ Spike Glycoprotein, Coronavirus - metabolism
/ Tea
