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Article

Molecular determinants of K36 binding in SARS-CoV-2 main protease revealed by MD simulations and alanine mutagenesis.

Journal of biomolecular structure & dynamics - 1 Aug 2026

AbouYoussef Mohamed L, El-Kelany Khaled E, Abdel Gaber Sara A, Aboelnga Mohamed M

Abstract excerpt

The SARS-CoV-2 main protease (Mpro) is a crucial target for antiviral drugs because of its vital function in viral polyprotein processing and replication. This study utilized molecular dynamics (MD) simulations to examine the binding stability and dynamic behavior of the inhibitor K36 with the wild-type (WT) Mpro and fifteen alanine-substituted versions that target functionally significant residues. The binding...

Read the complete abstract on PubMed

Topics

Molecular Dynamics Simulation
Alanine
Protein Binding
SARS-CoV-2
Hydrogen Bonding
Coronavirus 3C Proteases

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Mutation

Binding Sites

Viral Nonstructural Proteins

Catalytic Domain

Humans

Antiviral Agents

Mutagenesis

Ligands

Thermodynamics

Cysteine Endopeptidases

Protease Inhibitors

Source

Identifiers

PMID: 41733211
DOI: 10.1080/07391102.2026.2632174

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 20 Oct 2026.

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