Na+ CP type Iα 억제제

Regarding the chemical class Na+/K+-ATPase α1 inhibitors, these compounds are diverse but share a common feature in their ability to inhibit the function of the Na+/K+-ATPase enzyme. The inhibition process typically involves binding to the extracellular domain of the enzyme's α1 subunit, which prevents the enzyme from cycling between its phosphorylated (E2-P) and dephosphorylated (E1) states, essential for the active transport of sodium and potassium ions against their respective concentration gradients. This binding usually results in the stabilization of one of the enzyme's conformations, inhibiting the enzyme's activity.

The inhibitors listed include a variety of chemical structures, such as cardiotonic steroids and glycosides, which are naturally occurring compounds often found in plants. Most of these inhibitors, like ouabain and digoxin, bind to the same site on the enzyme, known as the cardiotonic steroid binding site. The interaction at this site is typically characterized by high affinity and specificity, leading to the powerful inhibition of the Na+/K+-ATPase activity. The inhibition of this enzyme affects the electrochemical gradient, which is critical for various cellular functions including cell volume regulation, secondary active transport, and electrical excitability of cells. With the ability to inhibit the Na+/K+-ATPase, these compounds can alter the ionic homeostasis of cells and consequently affect numerous physiological processes.