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        Native Mass Spectrometry and Covid-19: Uncovering Drug Binding and Oligomerization

        Many viruses are surrounded by lipid membranes, including SARS-CoV-2 and influenza. Both viruses contain viroporins, which are small, single-pass transmembrane proteins that oligomerize to form ion channels. The influenza M2 viroporin is already a clinically approved antiviral drug target. In other coronaviruses, the E protein viroporin which is involved with growth, could be a potential target for COVID-19 vaccine and antiviral development.

        In this webinar, Dr. Michael Marty will introduce the native mass spectrometry and lipid nanodisc technique as well as demonstrate how this approach can be used to directly measure the oligomeric state of protein and peptide complexes within intact model lipid bilayers.  Ongoing studies on the M2 and E protein will be discussed.

        What you will learn:

        • Latest advances in native MS for structural analysis of proteins
        • Native MS for the study of viral proteins and drug binding
        • Interfacing native MS with lipid nanodiscs to measure the oligomeric state of membrane protein and peptide complexes within intact model lipid bilayers

        About the presenter

        Michael Marty, Ph.D. Department of Chemistry & Biochemistry and Bio5 Institute, The University of Arizona

        Michael Marty, Ph.D. Department of Chemistry & Biochemistry and Bio5 Institute, The University of Arizona

        Michael Marty, Ph.D., is an Assistant Professor in the Department of Chemistry & Biochemistry and Bio5 Institute at The University of Arizona. His research applies lipoprotein nanodiscs with mass spectrometry to study membrane proteins, antimicrobial peptides, and their interactions with lipid bilayers. As the developer of UniDec, he is also interested in mass spectrometry data analysis and deconvolution.

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