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Related Experiment Video

Updated: Jan 11, 2026

High-throughput Confocal Imaging of Quantum Dot-Conjugated SARS-CoV-2 Spike Trimers to Track Binding and Endocytosis in HEK293T Cells
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Multimodal Structural Characterization of SARS-CoV-2 Spike Variants: Spectroscopic and Computational Insights.

Tiziana Mancini1, Nicole Luchetti2, Salvatore Macis1

  • 1Department of Physics, University La Sapienza, P.le A. Moro 2, 00185 Rome, Italy.

International Journal of Molecular Sciences
|November 13, 2025
PubMed
Summary

Mutations in SARS-CoV-2 spike protein subunit 1 alter its structure and function. This study analyzes three variants, revealing insights into viral adaptability and immune evasion for improved drug development.

Keywords:
ATR-IR spectroscopyCD spectroscopyMD simulationsSARS-CoV-2 variantshydrophilicitysecondary structurespike glycoproteins

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Area of Science:

  • Virology
  • Structural Biology
  • Biophysics

Background:

  • The SARS-CoV-2 pandemic has led to the emergence of numerous viral variants.
  • Mutations, especially in the spike glycoprotein, enhance viral adaptability and may alter protein structure and function.
  • Understanding these changes is crucial for combating the virus.

Purpose of the Study:

  • To perform the first systematic and comparative structural analysis of monomeric spike protein subunit 1 from three distinct SARS-CoV-2 variants.
  • To characterize the influence of specific mutations on the structural and functional properties of the spike protein.
  • To provide insights into viral infectivity, immune evasion, and potential therapeutic targets.

Main Methods:

  • Utilized a multimodal approach combining experimental and computational techniques.
  • Employed Attenuated Total Reflection Infrared and circular dichroism spectroscopies.
  • Conducted molecular dynamics simulations and surface polarity analyses at physiological pH (7.4).

Main Results:

  • Characterized the secondary structure composition, 3D conformational organization, and solvent interaction profiles of each variant.
  • Revealed how specific amino acid mutations influence the structural and functional properties of spike protein subunit 1.
  • Identified conformational changes and variations in solvent interactions linked to viral adaptability.

Conclusions:

  • Specific mutations in SARS-CoV-2 spike protein subunit 1 significantly impact its structure and function.
  • Observed conformational changes and altered solvent interactions have implications for viral infectivity and immune evasion.
  • Findings offer valuable insights for drug development, prevention strategies, and biosensor design against SARS-CoV-2 variants.