ArticleJournal of molecular recognition : JMR2012
Fluorescence correlation spectroscopy study of protein transport and dynamic interactions with clustered-charge peptide adsorbents.
Article in Journal of molecular recognition : JMR, 2012. 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 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.
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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, 26 citations in OpenAlex.
- Super-Resolving Particle Diffusion Heterogeneity in Porous Hydrogels via High-Speed 3D Active-Feedback Single-Particle Tracking Microscopy.Small (Weinheim an der Bergstrasse, Germany) · 2025Article
- Super-resolving particle diffusion heterogeneity in porous hydrogels via high-speed 3D active-feedback single-particle tracking microscopy.bioRxiv : the preprint server for biology · 2025Article
- Polymers for Disrupting Protein-Protein Interactions: Where Are We and Where Should We Be?Biomacromolecules · 2024Review
- Characterization of Porous Materials by Fluorescence Correlation Spectroscopy Super-resolution Optical Fluctuation Imaging.ACS nano · 2015Article
- Molecular approaches to chromatography using single molecule spectroscopy.Analytical chemistry · 2015Review
- High ionic strength narrows the population of sites participating in protein ion-exchange adsorption: a single-molecule study.Journal of chromatography. A · 2014Article
- Unified superresolution experiments and stochastic theory provide mechanistic insight into protein ion-exchange adsorptive separations.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- On the pH-responsive, charge-selective, polymer-brush-mediated transport probed by traditional and scanning fluorescence correlation spectroscopy.The journal of physical chemistry. B · 2013Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
Ion-exchange chromatography relies on electrostatic interactions between the adsorbent and the adsorbate and is used extensively in protein purification. Conventional ion-exchange chromatography uses ligands that are singly charged and randomly dispersed over the adsorbent, creating a heterogeneous distribution of potential adsorption sites. Clustered-charge ion exchangers exhibit higher affinity, capacity, and selectivity than their dispersed-charge counterparts of the same total charge density. In the present work, we monitored the transport behavior of an anionic protein near clustered-charge adsorbent surfaces using fluorescence correlation spectroscopy. We can resolve protein-free diffusion, hindered diffusion, and association with bare glass, agarose-coated, and agarose-clustered peptide surfaces, demonstrating that this method can be used to understand and ultimately optimize clustered-charge adsorbent and other surface interactions at the molecular scale.
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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.