Native MS and Ligand Observed NMR Uncovers Subtle SLiM Binding Variations that Mediate HSP90-Hop PPI Modulation | Synapse
May 8, 2026Open Access
Native MS and Ligand Observed NMR Uncovers Subtle SLiM Binding Variations that Mediate HSP90-Hop PPI Modulation
Key Points
The study aims to explore binding variations of peptides that mimic SLiM in HSP90 protein interactions.
Utilized native mass spectrometry (MS) and ligand observed NMR techniques.
Investigated the interaction of a non-natural tetrazole peptide with the HSP90 C-terminus.
Analyzed modulation effects on HSP90-Hop protein-protein interactions.
The tetrazole peptide effectively disrupted HSP90-Hop interactions.
Subtle variations in binding were observed, indicating potential for selective modulation.
Improvements in understanding SLiM interactions could enhance drug design strategies.
Abstract
We have previously demonstrated that a non-natural tetrazole containing peptide (2), which mimics the MEEVD Short Linear Motif (SLiM) found at the Heat Shock Protein 90 (HSP90) C-terminus, disrupts the...