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- 12Affinity
- 10Carbohydrates
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Quantifying protein-fatty acid interactions using electrospray ionization mass spectrometry
Download2011
Liu, Lan, Kitova, Elena N., Klassen, John S.
The application of the direct electrospray ionization mass spectrometry (ESI-MS) assay to quantify interactions between bovine β-lactoglobulin (Lg) and a series of fatty acids (FA), CH3(CH2)xCOOH, where x = 6 (caprylic acid, CpA), 8 (capric acid, CA), 10 (lauric acid, LA), 12 (myristic acid, MA),...
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Quantifying protein-fatty acid interactions using electrospray ionization mass spectrometry
Download2011
Klassen, John S., Kitova, Elena N., Liu, Lan
The application of the direct electrospray ionization mass spectrometry (ESI-MS) assay to quantify interactions between bovine β-lactoglobulin (Lg) and a series of fatty acids (FA), CH3(CH2)xCOOH, where x = 6 (caprylic acid, CpA), 8 (capric acid, CA), 10 (lauric acid, LA), 12 (myristic acid, MA),...
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2015
El-Hawiet, Amr, N. Kitova, Elena N., Klassen, John S.
The affinities of the most abundant oligosaccharides found in human milk for four bacterial exotoxins (from Vibrio cholerae and pathogenic Escherichia coli) were quantified for the first time. Association constants (Ka) for a library of 20 human milk oligosaccharides (HMOs) binding to Shiga toxin...
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2015
El-Hawiet, Amr, Klassen, John S., N. Kitova, Elena N.
The affinities of the most abundant oligosaccharides found in human milk for four bacterial exotoxins (from Vibrio cholerae and pathogenic Escherichia coli) were quantified for the first time. Association constants (Ka) for a library of 20 human milk oligosaccharides (HMOs) binding to Shiga toxin...
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Reliable determinations of protein-ligand interactions by direct ESI-MS measurements: Are we there yet?
Download2012
El-Hawiet, Amr, Klassen, John S., Kitova, Elena N., Schnier, Paul D.
The association-dissociation of noncovalent interactions between protein and ligands, such as other proteins, carbohydrates, lipids, DNA, or small molecules, are critical events in many biological processes. The discovery and characterization of these interactions is essential to a complete...
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Reliable determinations of protein-ligand interactions by direct ESI-MS measurements: Are we there yet?
Download2012
Klassen, John S., Kitova, Elena N., Schnier, Paul D., El-Hawiet, Amr
The association-dissociation of noncovalent interactions between protein and ligands, such as other proteins, carbohydrates, lipids, DNA, or small molecules, are critical events in many biological processes. The discovery and characterization of these interactions is essential to a complete...
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Screening anti-cancer drugs against tubulin using catch-and-release electrospray ionization mass spectrometry
Download2016
Kitova, Elena N., Klassen, John S., Winter, Philip, Tuszynski, Jack A., Darestani, Reza R.
Tubulin, which is the building block of microtubules, plays an important role in cell division. This critical role makes tubulin an attractive target for the development of chemotherapeutic drugs to treat cancer. Currently, there is no general binding assay for tubulin–drug interactions. The...
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Screening anti-cancer drugs against tubulin using catch-and-release electrospray ionization mass spectrometry
Download2016
Kitova, Elena N., Klassen, John S., Winter, Philip, Tuszynski, Jack A., Darestani, Reza R.
Tubulin, which is the building block of microtubules, plays an important role in cell division. This critical role makes tubulin an attractive target for the development of chemotherapeutic drugs to treat cancer. Currently, there is no general binding assay for tubulin–drug interactions. The...
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Screening carbohydrate libraries for protein interactions using the direct ESI-MS assay: Applications to libraries of unknown concentration
Download2014
El-Hawiet, Amr, Klassen, John S., Kitova, Elena N.
A semiquantitative electrospray ionization mass spectrometry (ESI-MS) binding assay suitable for analyzing mixtures of oligosaccharides, at unknown concentrations, for interactions with target proteins is described. The assay relies on the differences in the ratio of the relative abundances of...
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Screening carbohydrate libraries for protein interactions using the direct ESI-MS assay: Applications to libraries of unknown concentration
Download2014
El-Hawiet, Amr, Klassen, John S., Kitova, Elena N.
A semiquantitative electrospray ionization mass spectrometry (ESI-MS) binding assay suitable for analyzing mixtures of oligosaccharides, at unknown concentrations, for interactions with target proteins is described. The assay relies on the differences in the ratio of the relative abundances of...