WEBINAR

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

December 8, 2020 | 8 am PST, 11 am EST, 4 pm GMT & 5 pm CET 
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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.

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Webinar Summary

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 in growth, could be a potential target for COVID-19 vaccine and antiviral development. Although the oligomeric state of the M2 and E proteins are thought to be tetrameric and pentameric respectively, determining the oligomeric states of small transmembrane peptide complexes within membranes is challenging.

Native or non-denaturing mass spectrometry (MS) data suggests a more complex picture of the oligomeric state than previously assumed, highlighting the need for novel analytical methods to understand how these important biomedical targets interact within lipid membranes. This webinar will introduce the native MS and lipid nanodisc techniques and demonstrate how this 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.

 

Attend this webinar to discover:

  • 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

Speaker Information:


WebinarSpeakerImage
Michael Marty
Assistant Professor
Department of Chemistry and Biochemistry

University of Arizona