Comparative binding of two closely related dihydropyridines (isradipine and darodipine) to serum proteins and erythrocytes

Pharmacology. 1988;36(5):305-12. doi: 10.1159/000138399.

Abstract

The binding of the two drugs isradipine and darodipine, chemically related to dihydropyridines and potent calcium channel blockers, was studied in vitro to isolated plasma proteins, erythrocytes and human serum. The two drugs were strongly bound to serum proteins (up to 97%), mainly to human serum albumin (HSA), alpha 1-glycoprotein (AAG) and lipoproteins (VLDL, LDL and HDL). Their bindings to AAG were saturable with high affinity constants (isradipine 498,000 M-1, darodipine = 155,000 M-1; n = 1). The binding of these drugs to HSA, VLDL and HDL was unsaturable, but it was saturable on LDL. In blood the drugs partitioned in erythrocytes, 16% for isradipine and 14.8% for darodipine.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding, Competitive
  • Blood Proteins / metabolism*
  • Calcium Channel Blockers / blood*
  • Dihydropyridines / blood*
  • Erythrocytes / metabolism*
  • Humans
  • Isradipine
  • Lipoproteins / metabolism
  • Nifedipine / analogs & derivatives*
  • Nifedipine / blood
  • Pyridines / blood*
  • gamma-Globulins / metabolism

Substances

  • Blood Proteins
  • Calcium Channel Blockers
  • Dihydropyridines
  • Lipoproteins
  • Pyridines
  • gamma-Globulins
  • Nifedipine
  • darodipine
  • Isradipine