A native mass spectrometry approach to qualitatively elucidate interfacial epitopes of transient protein-protein interactions

Native mass spectrometric analysis of TPR2A and GrpE with unpurified peptides derived from limited proteolysis of their respective PPI partners (HSP90 C-terminus and DnaK) facilitated efficient, qualitative identification of interfacial epitopes involved in transient PPI formation. Application of th...

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Bibliographic Details
Published in:Chemical communications (Cambridge, England) England), 2024-05, Vol.6 (45), p.5844-5847
Main Authors: Veale, Clinton G. L, Chakraborty, Abir, Mhlanga, Richwell, Albericio, Fernando, de la Torre, Beatriz G, Edkins, Adrienne L, Clarke, David J
Format: Article
Language:English
Subjects:
Chemistry
Epitopes - chemistry
HSP70 Heat-Shock Proteins - chemistry
HSP70 Heat-Shock Proteins - metabolism
HSP90 Heat-Shock Proteins - chemistry
HSP90 Heat-Shock Proteins - metabolism
Mass Spectrometry
Peptides
Peptides - chemistry
Peptides - metabolism
Protein Binding
Proteins
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Summary:Native mass spectrometric analysis of TPR2A and GrpE with unpurified peptides derived from limited proteolysis of their respective PPI partners (HSP90 C-terminus and DnaK) facilitated efficient, qualitative identification of interfacial epitopes involved in transient PPI formation. Application of this approach can assist in elucidating interfaces of currently uncharacterised transient PPIs. Here we demonstrate a new approach in which native mass spectrometry and limited proteolysis is used in concert to rapidly identify interfacial peptides responsible for mediating a transient Protein-Protein Interaction.
ISSN:1359-7345
1364-548X
1364-548X
DOI:10.1039/d4cc01251h