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Understanding protein-drug interactions using ion mobility-mass spectrometry.
Eyers, Claire E; Vonderach, Matthias; Ferries, Samantha; Jeacock, Kiani; Eyers, Patrick A.
Afiliación
  • Eyers CE; Centre for Proteome Research, Institute of Integrative Biology, University of Liverpool, Liverpool L69 7ZB, United Kingdom; Department of Biochemistry, Institute of Integrative Biology, University of Liverpool, Liverpool L69 7ZB, United Kingdom. Electronic address: CEyers@Liverpool.ac.uk.
  • Vonderach M; Centre for Proteome Research, Institute of Integrative Biology, University of Liverpool, Liverpool L69 7ZB, United Kingdom; Department of Biochemistry, Institute of Integrative Biology, University of Liverpool, Liverpool L69 7ZB, United Kingdom.
  • Ferries S; Centre for Proteome Research, Institute of Integrative Biology, University of Liverpool, Liverpool L69 7ZB, United Kingdom; Department of Biochemistry, Institute of Integrative Biology, University of Liverpool, Liverpool L69 7ZB, United Kingdom.
  • Jeacock K; Department of Biochemistry, Institute of Integrative Biology, University of Liverpool, Liverpool L69 7ZB, United Kingdom.
  • Eyers PA; Department of Biochemistry, Institute of Integrative Biology, University of Liverpool, Liverpool L69 7ZB, United Kingdom.
Curr Opin Chem Biol ; 42: 167-176, 2018 02.
Article en En | MEDLINE | ID: mdl-29331721
Ion mobility-mass spectrometry (IM-MS) is an important addition to the analytical toolbox for the structural evaluation of proteins, and is enhancing many areas of biophysical analysis. Disease-associated proteins, including enzymes such as protein kinases, transcription factors exemplified by p53, and intrinsically disordered proteins, including those prone to aggregation, are all amenable to structural analysis by IM-MS. In this review we discuss how this powerful technique can be used to understand protein conformational dynamics and aggregation pathways, and in particular, the effect that small molecules, including clinically-relevant drugs, play in these processes. We also present examples of how IM-MS can be used as a relatively rapid screening strategy to evaluate the mechanisms and conformation-driven aspects of protein:ligand interactions.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas Quinasas / Espectrometría de Masas / Preparaciones Farmacéuticas / Proteínas / Proteínas Intrínsecamente Desordenadas / Espectrometría de Movilidad Iónica Límite: Humans Idioma: En Revista: Curr Opin Chem Biol Asunto de la revista: BIOQUIMICA Año: 2018 Tipo del documento: Article Pais de publicación: Reino Unido

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas Quinasas / Espectrometría de Masas / Preparaciones Farmacéuticas / Proteínas / Proteínas Intrínsecamente Desordenadas / Espectrometría de Movilidad Iónica Límite: Humans Idioma: En Revista: Curr Opin Chem Biol Asunto de la revista: BIOQUIMICA Año: 2018 Tipo del documento: Article Pais de publicación: Reino Unido