Plant-Derived Antimicrobial Peptide Inhibitor against the Main Protease of SARS-CoV-2
Disciplines
Biochemistry
Abstract (300 words maximum)
The SARS-CoV-2 virus represented a significant threat to the health of people across the globe, with 7.03 million deaths and 774.6 million infections caused by the virus. This is a positive sense single-stranded RNA (+ssRNA) virus which translates 29 proteins in the host cell. Among these proteins, scientists have identified crucial proteins such as the 3-chymotrypsin-like protease, main protease (Mpro), which performs a very critical function in viral replication and transcription. Various reliable and effective methods were developed to screen small molecules and peptide inhibitors targeting the catalytic dyad, C145 and H41, of the main protease. The focused peptide of this experiment is Ib-AMP-3, which is derived from the seeds of Impatiens balsamina, and has shown activity as an anti-gram+ and antifungal peptide. The determination for this peptide’s binding affinity was identified using HDock software targeting the catalytic dyad and surrounding residues of Mpro resulting in a binding affinity of -234.57. The peptide was synthesized utilizing a Liberty Blue 2.0 Microwave Peptide Synthesis, and its synthesis was confirmed by running the sample through a LTQ XL Linear Ion Trap Mass Spectrometer which identified the peptide with a mass to charge ration (m/z) of 512.83 [M+H]+5 Da, 640.50 [M+H]+4 Da, and 853.33 [M+H]+3 Da. The 50% inhibitory concentration (IC50) value will be determined using a selected ion monitoring (SIM) coupled with liquid chromatography-mass spectroscopy (LC-MS) assay. This project was conducted as a CURE research project that meets once a week in lab for a three-hour period.
Academic department under which the project should be listed
CSM - Chemistry and Biochemistry
Primary Investigator (PI) Name
Mohammed A Halim
Plant-Derived Antimicrobial Peptide Inhibitor against the Main Protease of SARS-CoV-2
The SARS-CoV-2 virus represented a significant threat to the health of people across the globe, with 7.03 million deaths and 774.6 million infections caused by the virus. This is a positive sense single-stranded RNA (+ssRNA) virus which translates 29 proteins in the host cell. Among these proteins, scientists have identified crucial proteins such as the 3-chymotrypsin-like protease, main protease (Mpro), which performs a very critical function in viral replication and transcription. Various reliable and effective methods were developed to screen small molecules and peptide inhibitors targeting the catalytic dyad, C145 and H41, of the main protease. The focused peptide of this experiment is Ib-AMP-3, which is derived from the seeds of Impatiens balsamina, and has shown activity as an anti-gram+ and antifungal peptide. The determination for this peptide’s binding affinity was identified using HDock software targeting the catalytic dyad and surrounding residues of Mpro resulting in a binding affinity of -234.57. The peptide was synthesized utilizing a Liberty Blue 2.0 Microwave Peptide Synthesis, and its synthesis was confirmed by running the sample through a LTQ XL Linear Ion Trap Mass Spectrometer which identified the peptide with a mass to charge ration (m/z) of 512.83 [M+H]+5 Da, 640.50 [M+H]+4 Da, and 853.33 [M+H]+3 Da. The 50% inhibitory concentration (IC50) value will be determined using a selected ion monitoring (SIM) coupled with liquid chromatography-mass spectroscopy (LC-MS) assay. This project was conducted as a CURE research project that meets once a week in lab for a three-hour period.