ArticleJournal of medicinal chemistry2021
A Crowding Barrier to Protein Inhibition in Colloidal Aggregates.
Article in Journal of medicinal chemistry, 2021. 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
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed.
- Article
- Library docking for Cannabinoid-2 Receptor ligands.bioRxiv : the preprint server for biology · 2026Article
- Drug-induced phospholipidosis as an artifact in antiviral drug repurposing.bioRxiv : the preprint server for biology · 2025Article
- Advancing promiscuous aggregating inhibitor analysis with intelligent machine learning classification.Briefings in bioinformatics · 2025Article
- The Potential of Congo Red Supplied Aggregates of Multitargeted Tyrosine Kinase Inhibitor (Sorafenib, BAY-43-9006) in Enhancing Therapeutic Impact on Bladder Cancer.International journal of molecular sciences · 2023Article
- Large library docking for novel SARS-CoV-2 main protease non-covalent and covalent inhibitors.Protein science : a publication of the Protein Society · 2023Article
- Photodynamic Activity of TMPyP4/TiOPharmaceutics · 2023Article
- Colloidal Aggregators in Biochemical SARS-CoV-2 Repurposing Screens.Journal of medicinal chemistry · 2021Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Small molecule colloidal aggregates adsorb and partially denature proteins, inhibiting them artifactually. Oddly, this inhibition is typically time-dependent. Two mechanisms might explain this: low concentrations of the colloid and enzyme might mean low encounter rates, or colloid-based protein denaturation might impose a kinetic barrier. These two mechanisms should have different concentration dependencies. Perplexingly, when enzyme concentration was increased, incubation times actually lengthened, inconsistent with both models and with classical chemical kinetics of solution species. We therefore considered molecular crowding, where colloids with lower protein surface density demand a shorter incubation time than more crowded colloids. To test this, we grew and shrank colloid surface area. As the surface area shrank, the incubation time lengthened, while as it increased, the converse was true. These observations support a crowding effect on protein binding to colloidal aggregates. Implications for drug delivery and for detecting aggregation-based inhibition will be discussed.
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Registered trials
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