ArticleiScience2021
High-throughput determination of protein affinities using unmodified peptide libraries in nanomolar scale.
Article in iScience, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Orthogonal Temperature-Related Intensity Change and Time-Resolved Förster Resonance Energy Transfer High-Throughput Screening Platform for the Discovery of SLIT2 Binders.Bio-protocol · 2026Article
- High-throughput investigation of macromolecular interactions for drug development using spectral shift technology.Biophysical reviews · 2025Review
- Target Engagement Assays in Early Drug Discovery.Journal of medicinal chemistry · 2025Review
- Milestone Review: Unlocking the Proteomics of Glycine Receptor Complexes.Journal of neurochemistry · 2025Review
- Inhibition of the YAP-MMB interaction and targeting NEK2 as potential therapeutic strategies for YAP-driven cancers.Oncogene · 2024Article
- Startle Disease: New Molecular Insights into an Old Neurological Disorder.The Neuroscientist : a review journal bringing neurobiology, neurology and psychiatry · 2023Review
- Molecular characterization of AIFM2/FSP1 inhibition by iFSP1-like molecules.Cell death & disease · 2023Article
- Peptide Microarrays for Studying Autoantibodies in Neurological Disease.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Multivalent binding kinetics resolved by fluorescence proximity sensing.Communications biology · 2022Article
- A FeFrontiers in molecular biosciences · 2022Article
- Low-cost synthesis of peptide libraries and their use for binding studies via temperature-related intensity change.STAR protocols · 2021Article
- Combining flavin photocatalysis with parallel synthesis: a general platform to optimize peptides with non-proteinogenic amino acids.Chemical science · 2021Article
- Conformational Plasticity of Hepatitis B Core Protein Spikes Promotes Peptide Binding Independent of the Secretion Phenotype.Microorganisms · 2021Article
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein-protein interactions (PPIs) are of fundamental importance for our understanding of physiology and pathology. PPIs involving short, linear motifs play a major role in immunological recognition, signaling, and regulation and provide attractive starting points for pharmaceutical intervention. Yet, state-of-the-art protein-peptide affinity determination approaches exhibit limited throughput and sensitivity, often resulting from ligand immobilization, labeling, or synthesis. Here, we introduce a high-throughput method for in-solution analysis of protein-peptide interactions using a phenomenon called temperature related intensity change (TRIC). We use TRIC for the identification and fine-mapping of low- and high-affinity protein interaction sites and the definition of sequence binding requirements. Validation is achieved by microarray-based studies using wild-type and mutated recombinant protein and the native protein within tissue lysates. On-chip neutralization and strong correlation with structural data establish TRIC as a quasi-label-free method to determine binding affinities of unmodified peptide libraries with large dynamic range.
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