ArticleACS chemical biology2019
Site-Resolved and Quantitative Characterization of Very Weak Protein-Ligand Interactions.
Article in ACS chemical biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The trial behind it
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Who cites it
8 citing papers in PubMed.
- Advances in utilizing reverse micelles to investigate membrane proteins.Biochemical Society transactions · 2024Review
- Ligandability at the Membrane Interface of GPx4 Revealed through a Reverse Micelle Fragment Screening Platform.JACS Au · 2024Article
- An NMR Approach for Investigating Membrane Protein-Lipid Interactions Using Native Reverse Micelles.Bio-protocol · 2024Article
- Ligandability at the membrane interface of GPx4 revealed through a reverse micelle fragment screening platform.bioRxiv : the preprint server for biology · 2024Article
- Profiling of ERBB receptors and downstream pathways reveals selectivity and hidden properties of ERBB4 antagonists.iScience · 2024Article
- Investigating protein-membrane interactions using native reverse micelles constructed from naturally sourced lipids.Protein science : a publication of the Protein Society · 2023Article
- Carnitine is a pharmacological allosteric chaperone of the human lysosomalJournal of enzyme inhibition and medicinal chemistry · 2021Article
- Extending the Detection Limit in Fragment Screening of Proteins Using Reverse Micelle Encapsulation.ACS chemical biology · 2019Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Very weak interactions between small organic molecules and proteins have long been predicted and are expected to have dissociation constants of hundreds of millimolar and above. Unfortunately, quantitative evaluation of binding in a high-resolution structural context for this affinity regime is particularly difficult and often impossible using existing experimental approaches. Here, we show that nanoscale encapsulation of single protein molecules within the water core of reverse micelles enables the detection and evaluation of weak binding interactions at atomic resolution using solution NMR spectroscopy. This strategy is used to survey the interactions of a set of small molecules with the cytokine interleukin-1β (IL-1β). The interaction of IL-1β with these molecules is found to vary from more diffuse and weak binding modes to more specific and with a relatively higher affinity. The interactions detected here cover a large portion of the protein surface and have dissociation constants mostly in the low molar range. These results illustrate the ability of a protein to interact productively with a variety of small molecule functional groups and point to a broader potential to target even relatively featureless protein surfaces for applications in chemical biology and drug discovery.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.