Understanding SARS Proteinase Binding with Octapeptides
Author Information
Author(s): Phakthanakanok Krongsakda, Ratanakhanokchai Khanok, Kyu Khin Lay, Sompornpisut Pornthep, Watts Aaron, Pinitglang Surapong
Primary Institution: King Mongkut's University of Technology Thonburi
Hypothesis
Glu47 of SARS CoVMpro is an important residue in the S3 subsite and is involved in binding with P3Lys of the octapeptide.
Conclusion
The study found that Glu47 plays a key role in the binding of octapeptides to the SARS CoVMpro enzyme.
Supporting Evidence
- The S3 subsite of the enzyme had a negatively charged region due to the presence of Glu47.
- MD simulations showed that Glu47 plays a key role in electrostatic bonding with the P3Lys of the octapeptide.
- The octapeptide P3Lys had the lowest docking energy, indicating it was the most specific for the enzyme.
Takeaway
This research shows that a specific part of a virus enzyme helps it grab onto certain pieces of protein, which is important for making medicines.
Methodology
The study used molecular docking and molecular dynamics simulations to analyze the interactions between SARS CoVMpro and octapeptides.
Digital Object Identifier (DOI)
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