ArticleACS chemical biology2017
Internal Structure and Preferential Protein Binding of Colloidal Aggregates.
Article in ACS chemical biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
17 citing papers in PubMed, 30 citations in OpenAlex.
- Article
- Supramolecular dye nanoassemblies for advanced diagnostics and therapies.Bioengineering & translational medicine · 2024Review
- Molecular dynamics simulations as a guide for modulating small molecule aggregation.Journal of computer-aided molecular design · 2024Article
- 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
- Fragment-based drug nanoaggregation reveals drivers of self-assembly.Nature communications · 2023Article
- Lies and Liabilities: Computational Assessment of High-Throughput Screening Hits to Identify Artifact Compounds.Journal of medicinal chemistry · 2023Article
- Discovery of Kinase and Carbonic Anhydrase Dual Inhibitors by Machine Learning Classification and Experiments.Pharmaceuticals (Basel, Switzerland) · 2022Article
- Hydroxamic Acid as a Potent Metal-Binding Group for Inhibiting Tyrosinase.Antioxidants (Basel, Switzerland) · 2022Article
- Probing the free-state solution behavior of drugs and their tendencies to self-aggregate into nano-entities.Nature protocols · 2021Review
- Gains from no real PAINS: Where 'Fair Trial Strategy' stands in the development of multi-target ligands.Acta pharmaceutica Sinica. B · 2021Review
- Preparing (Metalla)carboranes for Nanomedicine.ChemMedChem · 2021Review
- A Crowding Barrier to Protein Inhibition in Colloidal Aggregates.Journal of medicinal chemistry · 2021Article
- Merging Ligand-Based and Structure-Based Methods in Drug Discovery: An Overview of Combined Virtual Screening Approaches.Molecules (Basel, Switzerland) · 2020Review
- Protein Stability Effects in Aggregate-Based Enzyme Inhibition.Journal of medicinal chemistry · 2019Article
- Computational advances in combating colloidal aggregation in drug discovery.Nature chemistry · 2019Review
- Effect of tolytoxin on tunneling nanotube formation and function.Scientific reports · 2019Article
- Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
Colloidal aggregates of small molecules are the most common artifact in early drug discovery, sequestering and inhibiting target proteins without specificity. Understanding their structure and mechanism has been crucial to developing tools to control for, and occasionally even exploit, these particles. Unfortunately, their polydispersity and transient stability have prevented exploration of certain elementary properties, such as how they pack. Dye-stabilized colloidal aggregates exhibit enhanced homogeneity and stability when compared to conventional colloidal aggregates, enabling investigation of some of these properties. By small-angle X-ray scattering and multiangle light scattering, pair distance distribution functions suggest that the dye-stabilized colloids are filled, not hollow, spheres. Stability of the coformulated colloids enabled investigation of their preference for binding DNA, peptides, or folded proteins, and their ability to purify one from the other. The coformulated colloids showed little ability to bind DNA. Correspondingly, the colloids preferentially sequestered protein from even a 1600-fold excess of peptides that are themselves the result of a digest of the same protein. This may reflect the avidity advantage that a protein has in a surface-to-surface interaction with the colloids. For the first time, colloids could be shown to have preferences of up to 90-fold for particular proteins over others. Loaded onto the colloids, bound enzyme could be spun down, resuspended, and released back into buffer, regaining most of its activity. Implications of these observations for colloid mechanisms and utility will be considered.
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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.