Project Title

Designing Potent Antiviral Peptide Inhibitors Targeting the Spike Protein and Angiotensin-Converting Enzyme-2

Academic department under which the project should be listed

CSM - Chemistry and Biochemistry

Faculty Sponsor Name

Mohammad A. Halim

Abstract (300 words maximum)

The Covid-19 pandemic has become a serious global issue since its discovery in December of 2019. SARS-CoV-2 virus is highly contagious and has killed over 5.3 million people in the world. The current FDA approved vaccines are effective; however, they lose their effectiveness after a few months of receiving both doses of the vaccine, and it is recommended to get a booster shot six months after receiving the second dose. Due to this, new and effective antiviral therapeutic treatments are being sought out to create an alternative treatment for SARS-CoV-2’svariants. Various studies confirmed that SARS-CoV-2 spreads faster with greater infectivity than other coronaviruses, partly due to its elevated binding affinity to angiotensin-converting enzyme-2 (ACE-2). The interaction between the spike protein (S) of the virus and the ACE2 receptor is the critical route of entry for the virus. Therefore, the S-ACE2 complex is a potential target for drug or vaccine development. Small molecules or peptides can be designed as therapeutics that will disrupt the interaction between the S-ACE2 complex; however, small molecules are not ideal for targeting large protein-protein interactions. In this study, 29 antiviral peptides were screened to identify the best candidates using a computational approach. Molecular docking results showed that the Gibbs free energy of these peptides ranges from -36.43 kcal/mol to -67.01 kcal/mol. Among these peptides, three showed the highest Gibbs free energy around -60 kcal/mol and strong interactions with the residues in the interface of the S-ACE2 complex. Hydrogen bonding and hydrophobic interactions play important roles for the interactions between peptides and S-ACE2 complex. Relatively small size peptides were synthesized and characterized by HPLC and mass spectrometry. This study provides a guide designing and optimizing the most effective peptides targeting the S-ACE2 complex.

Disciplines

Analytical Chemistry | Biochemistry | Bioinformatics | Medicinal-Pharmaceutical Chemistry | Other Immunology and Infectious Disease

Project Type

Poster

How will this be presented?

Yes, in person

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Designing Potent Antiviral Peptide Inhibitors Targeting the Spike Protein and Angiotensin-Converting Enzyme-2

The Covid-19 pandemic has become a serious global issue since its discovery in December of 2019. SARS-CoV-2 virus is highly contagious and has killed over 5.3 million people in the world. The current FDA approved vaccines are effective; however, they lose their effectiveness after a few months of receiving both doses of the vaccine, and it is recommended to get a booster shot six months after receiving the second dose. Due to this, new and effective antiviral therapeutic treatments are being sought out to create an alternative treatment for SARS-CoV-2’svariants. Various studies confirmed that SARS-CoV-2 spreads faster with greater infectivity than other coronaviruses, partly due to its elevated binding affinity to angiotensin-converting enzyme-2 (ACE-2). The interaction between the spike protein (S) of the virus and the ACE2 receptor is the critical route of entry for the virus. Therefore, the S-ACE2 complex is a potential target for drug or vaccine development. Small molecules or peptides can be designed as therapeutics that will disrupt the interaction between the S-ACE2 complex; however, small molecules are not ideal for targeting large protein-protein interactions. In this study, 29 antiviral peptides were screened to identify the best candidates using a computational approach. Molecular docking results showed that the Gibbs free energy of these peptides ranges from -36.43 kcal/mol to -67.01 kcal/mol. Among these peptides, three showed the highest Gibbs free energy around -60 kcal/mol and strong interactions with the residues in the interface of the S-ACE2 complex. Hydrogen bonding and hydrophobic interactions play important roles for the interactions between peptides and S-ACE2 complex. Relatively small size peptides were synthesized and characterized by HPLC and mass spectrometry. This study provides a guide designing and optimizing the most effective peptides targeting the S-ACE2 complex.

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