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Sensing Dynamically Evolved Short-Range Nanomechanical Forces in Fast-Mutating Single Viral Spike Proteins.

Amir Farokh Payam1,2, Riccardo Funari3,4, Gaetano Scamarcio3,4

  • 1Nanotechnology and Integrated Bioengineering Centre (NIBEC) School of Engineering Ulster University York Street Belfast, Northern Ireland, BT15 1AP UK.

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Summary

This study quantifies the nanomechanical properties of SARS-CoV-2 spike proteins from various variants. Understanding these mechanical changes linked to mutations aids in developing new antiviral strategies.

Keywords:
Hamakar constantnanomechanicssingle-proteinsviruses

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Area of Science:

  • Biophysics
  • Virology
  • Materials Science

Background:

  • Viral mutations, particularly in spike proteins, drive the evolution of viruses like SARS-CoV-2.
  • Understanding the mechanical properties of viral proteins is crucial for developing targeted antiviral therapies.

Purpose of the Study:

  • To quantify the chemomechanical features of single spike proteins from SARS-CoV-2 alpha, beta, and gamma variants.
  • To correlate these nanomechanical properties with specific point mutations.
  • To explore new avenues for understanding viral protein function and evolution.

Main Methods:

  • Utilized amplitude-modulation atomic force microscopy (AM-AFM) with dynamic force-distance curve (FDC) spectroscopy.
  • Integrated theoretical models for comprehensive analysis.
  • Quantified Young's modulus, stiffness, adhesion forces, van der Waals forces, and dissipative energy.

Main Results:

  • Successfully quantified key nanomechanical properties of single spike proteins from different SARS-CoV-2 variants.
  • Established a correlation between specific mutations and alterations in protein mechanical characteristics.
  • Demonstrated the utility of single-protein nanomechanical measurements.

Conclusions:

  • Nanomechanical profiling of viral proteins offers insights into mutation-driven functional changes.
  • This approach provides a foundation for developing novel inhibitory strategies against evolving viruses.
  • Single-protein nanomechanics can advance the understanding of viral evolution and protein biochemistry.