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Engineering Antiviral Agents via Surface Plasmon Resonance
Published on: June 14, 2022
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A Rationally Designed Synthetic Antiviral Peptide Binder Targeting the Receptor-Binding Domain of SARS-CoV-2
Lalita Mohan Behera1, Pulkit Kr Gupta1, Manaswini Ghosh1
1Chemical Biology Laboratory, School of Basic Sciences, Indian Institute of Technology Bhubaneswar, Bhubaneswar 752050, Odisha, India.
The Journal of Physical Chemistry. B
|April 24, 2024
Summary
A novel designer peptide, SR16, effectively binds to SARS-CoV-2's spike protein, offering a potential new antiviral strategy. This peptide shows promise for preventing viral entry and warrants further development for COVID-19 treatment.
Area of Science:
- Biochemistry
- Virology
- Drug Discovery
Background:
- Severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) causes the COVID-19 pandemic.
- Viral entry relies on interactions between the SARS-CoV-2 spike protein's receptor-binding domain (RBD) and human ACE2 receptors.
- Developing alternative therapeutics is crucial due to vaccine limitations and viral resurgence.
Purpose of the Study:
- To design and characterize a novel peptide inhibitor targeting the SARS-CoV-2 RBD-ACE2 interaction.
- To evaluate the peptide's binding affinity, stability, and safety profile.
Main Methods:
- Design and synthesis of a short, non-peptidic peptide (SR16).
- Biophysical studies to assess binding affinity and conformation.
- In vitro assays for trypsin degradation, mammalian cell toxicity, and hemolysis.
Main Results:
- SR16, a ≤18 amino acid peptide, exhibits a helical structure and high-affinity binding to the SARS-CoV-2 RBD.
- The peptide is resistant to trypsin degradation.
- SR16 demonstrates no toxicity to mammalian cells or hemolysis in human erythrocytes.
Conclusions:
- SR16 is a promising peptide binder for the SARS-CoV-2 RBD.
- SR16 has potential for development as a SARS-CoV-2 antiviral agent.
- Further optimization and development are recommended.
