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Affinity Measurement of Non-covalent Interactions of the Covalent KRAS G12C GDP Inhibitor MRTX849 to RAS Isoforms Using Surface Plasmon Resonance

  1. Author:
    Alexander,Patrick
    Stephen,Andy

  2. Author Address

    NCI RAS Initiative, Cancer Research Technology Program, Frederick National Laboratory for Cancer Research, Frederick, MD, USA. patrick.alexander@nih.gov.,
    1. Year: 2024
  2. Journal: Methods in Molecular Biology (Clifton, N.J.)
    1. 2797
    2. Pages: 103-114
  4. Type of Article: Article
  1. Abstract:

    Surface plasmon resonance (SPR) is an optical effect at an electron-rich surface that enables affinity measurements of biomolecules in real time. It is label free and versatile, not limited to proteins, nucleic acids, and small molecules. SPR is a widely accepted method to measure not only affinity of molecular interactions but also association and dissociation rates of such interactions. In this chapter, we describe a general method to measure the affinity of a small molecule drug, MRTX849, to GDP bound HRAS, KRAS, and NRAS. © 2024. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.

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External Sources

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  2. DOI: 10.1007/978-1-0716-3822-4_8
  3. PMID: 38570455

Library Notes

  1. Fiscal Year: FY2023-2024
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