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ACE2 Peptide Fragment Interaction with Different S1 Protein Sites.

Aleksei Kuznetsov1, Piret Arukuusk2, Heleri Härk2

  • 1Institute of Chemistry, University of Tartu, Tartu, Estonia.

International Journal of Peptide Research and Therapeutics
|December 6, 2021
PubMed
Summary

A peptide targeting the ACE2 receptor binding site inhibits SARS-CoV-2 (coronavirus) spike protein S1 binding. This peptide stabilizes the S1-ACE2 complex, suggesting new antiviral strategies targeting virus-host interactions.

Keywords:
ACE2 peptide fragmentAllosteric binding siteBio-layer interferometryPeptidePeptide binding kineticsPeptide dockingSARS-CoV-2 spike protein

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Area of Science:

  • Biochemistry
  • Virology
  • Molecular Biology

Background:

  • SARS-CoV-2 (coronavirus) utilizes its spike protein S1 to bind angiotensin-converting enzyme 2 (ACE2) on host cells for viral entry.
  • The ACE2 α1 domain contains the primary binding site for the SARS-CoV-2 S1 protein.

Purpose of the Study:

  • To investigate the effect of a specific peptide (QAKTFLDKFNHEAEDLFYQ) on the kinetics of SARS-CoV-2 spike protein S1 binding to ACE2.
  • To characterize the interaction mechanism between the virus and its host cell, aiming to identify novel antiviral intervention strategies.

Main Methods:

  • Bio-layer interferometry was employed to measure the kinetics of S1-ACE2 complex formation in the presence of varying peptide concentrations.
  • Kinetic analysis of S1-ACE2 complex dissociation was performed after preincubation of the peptide with either S1 protein or ACE2.

Main Results:

  • The peptide QAKTFLDKFNHEAEDLFYQ inhibited the formation of the S1-ACE2 complex when preincubated with the S1 protein.
  • Preincubation of the peptide with S1 protein led to stabilization of the S1-ACE2 complex, with effects dependent on peptide concentration and preincubation time.
  • Computational mapping revealed two additional binding sites on the S1 protein surface, distinct from the main receptor-binding domain.

Conclusions:

  • The findings suggest the formation of a ternary complex involving S1, ACE2, and the peptide, indicating potential allosteric modulation or alternative binding sites.
  • The study highlights the potential of short, peptide-derived inhibitors for developing new strategies to combat viral infections by disrupting virus-host interactions.