Max Planck Society is reporting that scientists from the Max Planck Institute for Biophysical Chemistry in Göttingen, working together with researchers from the Institute for Neural Signal Processing in Hamburg and French colleagues from the University of Marseille are uncovering how toxins combine with cellular potassium channels and change their structure. This work might lead to a development of new classes of medications for a variety of diseases, such as hypertension. Investigators, that reported their work in the latest Nature, used solid-state NMR to look at the action of poison from the north African scorpion Androctonus mauretanicus mauretanicus on potassium channel:
The researchers first examined the electrophysiological characteristics of the “poisoned” channel protein. The scientists “spin-marked” some of them and investigated them with solid-state NMR. Spin-marked proteins contain carbon and nitrogen atoms with an intrinsic magnetic moment (spin) which strengthens the NMR’s signals. Looking at spectroscopic data before and after the toxin affected the channel, it turned out that the poison attaches to a particular area of the channel – the pore region – and changes the area’s structure. The poison is thus only effective when it recognises a particular amino acid sequence in the ion channel. It is also important how intrinsically flexible the binding partner is; for a strong interaction to take place, the molecules of both partners have to be able to change their structures.
Applying these new spectroscopic methods, scientists are now better understanding the pharmacology and physiology of potassium channels. This could lead to better, more specific medications.
The press release…