ArticleElectrophoresis2010
Free-solution interaction assay of carbonic anhydrase to its inhibitors using back-scattering interferometry.
Article in Electrophoresis, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Quantitative Characterization of Three Carbonic Anhydrase Inhibitors by LESA Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2022Article
- Ultra Stable Molecular Sensors by Submicron Referencing and Why They Should Be Interrogated by Optical Diffraction-Part II. Experimental Demonstration.Sensors (Basel, Switzerland) · 2020Article
- Membrane Association Dictates Ligand Specificity for the Innate Immune Receptor NOD2.ACS chemical biology · 2017Article
- Therapeutic Delivery of HJournal of the American Chemical Society · 2016Article
- Back-scattering interferometry: an ultrasensitive method for the unperturbed detection of acetylcholinesterase-inhibitor interactions.Angewandte Chemie (International ed. in English) · 2012Article
- Interferometric methods for label-free molecular interaction studies.Analytical chemistry · 2012Review
- Histone demethylase LSD1 is a folate-binding protein.Biochemistry · 2011Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Back-scattering interferometry (BSI) is a label-free, free-solution, small-volume technique used for characterizing binding interactions, which is also relevant to a growing number of biosensing applications including drug discovery. Here, we use BSI to characterize the interaction of carbonic anhydrase enzyme II with five well-known carbonic anhydrase enzyme II inhibitors (± sulpiride, sulfanilamide, benzene sulfonamide, dansylamide, and acetazolamide) in the presence of DMSO. Dissociation constants calculated for each interaction were consistent with literature values previously obtained using surface plasmon resonance and fluorescence-based competition assays. Results demonstrate the potential of BSI as a drug-screening tool which is fully compatible with DMSO and does not require immobilization or labeling, therefore allowing binding interactions to be characterized in the native state. BSI has the potential for reducing labor costs, sample consumption, and assay time while providing enhanced reliability over existing techniques.
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Registered trials
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