Phage Display-Derived Peptide for the Specific Binding of SARS-CoV-2

Area of Science:

• Biotechnology
• Virology
• Molecular Biology

Background:

• The COVID-19 pandemic caused by SARS-CoV-2 remains a global health crisis.
• Limited vaccine production and rapid viral evolution necessitate complementary diagnostic and therapeutic strategies.
• Phage display peptide libraries offer a method for identifying novel antigen-specific peptides.

Purpose of the Study:

• To screen a 12-mer phage display peptide library against the SARS-CoV-2 receptor-binding domain (RBD).
• To identify and characterize peptides with specific binding affinity to SARS-CoV-2.
• To evaluate the potential of identified peptides for developing diagnostic tools.

Main Methods:

• Screening of a 12-mer phage display peptide library against SARS-CoV-2 RBD.
• Enzyme-linked immunosorbent assay (ELISA) to assess peptide-RBD binding.
• Surface plasmon resonance (SPR) to determine binding affinity (Kd).
• Transmission electron microscopy (TEM) and magnetic bead assay to confirm binding to inactivated SARS-CoV-2 virus.

Main Results:

• Five peptides demonstrated binding to the SARS-CoV-2 RBD via ELISA.
• Peptide no. 1 exhibited specific binding to SARS-CoV-2 RBD with a Kd of 5.8 μM, confirmed by SPR.
• TEM and magnetic bead assays confirmed that peptide no. 1 specifically binds to inactivated SARS-CoV-2 virus.

Conclusions:

• A SARS-CoV-2-specific peptide was identified using phage display technology.
• The identified peptide demonstrates high binding affinity and specificity for the virus.
• This peptide holds significant potential as a bioreceptor for rapid and accurate SARS-CoV-2 detection.