Oral Sessions (Day1, Day2, Day3)
Poster Presentations (Day1, Day2, Day3)
Poster Presentations
- Day 2, June 23（Thu.） Room P (501, 502 and 503)
-
2P-04 PDF
Assaying Protein / Ligand Binding with High Resolution Native Mass Spectrometry
An increase in the number of candidates for drug and therapeutic candidates is happening in all pharmaceutical and research environments as mass spectrometry capabilities increase. However, the ability to process the data has not kept up. Protein Metrics has created software to automate and speed up this process to reduce the burden on scientists and to make sure that the raw data is turned into information faster.
Carbonic anhydrase (CA) catalyzes the reversible reaction
CO2 + H2O ↔ HCO3- +H+
CA is especially well suited as a model enzyme for biophysical studies of protein / ligand binding1) because it is inexpensive, well characterized, and medically relevant (in glaucoma, obesity, and altitude sickness). CA inhibitors, primarily aryl sulfonamides, are also well understood and readily available.
Here we use CA as a model enzyme for protein / ligand binding study with high resolution native mass spectrometry (nMS). There are a number of technologies for protein / ligand screening, including fluorescent or radioactive labeling, surface plasmon resonance spectroscopy, circular dichroism, and isothermal titration calorimetry.
Relative to these methods, nMS offers some advantages: no need for chemical tags, observation of multiple and nonspecific binding, and direct identification of ligands in competitive binding experiments.
Reference
1) V M. Krishnamurthy et a l., Chem Rev 2008 108(3): 946-1051