Department of Physical Chemistry and Technology of Polymers, Section of Physics and Applied Mathematics, Silesian University of Technology, Ks. M. Strzody 9, 44-100 Gliwice, Poland. Electronic address: [Email]
Using the results from previous modeling of the ball and chain inactivation of the potassium channels we try to model the inactivation of the NaV 1.5 sodium channels in adult and neonatal form. The (fast) inactivation of sodium channels differs from the inactivation of the potassium channels by the use of a inactivating hinge rather than a ball on a chain. The adult and neonatal variants of the channel differ mostly in a charged amino acid residue located on the extracellular side. We show that a drift caused by this residue is sufficient to describe the differences in inactivation between the two forms of the NaV 1.5. We use the survival probability, the patch-clamp measurable parameter, to discriminate between the cells of different metastaticity.
