Binding of a dihydropyridine felodipine-analogue to calmodulin and related calcium-binding proteins.
Article Details
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Bostrom SL, Westerlund C, Rochester S, Vogel HJ
Binding of a dihydropyridine felodipine-analogue to calmodulin and related calcium-binding proteins.
Biochem Pharmacol. 1988 Oct 1;37(19):3723-8.
- PubMed ID
- 3178884 [ View in PubMed]
- Abstract
A dihydropyridine-affinity column was prepared by coupling a physiologically active and vasoselective amino-derivative of felodipine to divinylsulfone-activated Trisacryl GF2000. Calmodulin (CaM) as well as the homologous calcium-binding proteins skeletal and cardiac Troponin C (sTnC and cTnC) and S100b bound to this resin in a calcium-dependent manner. In contrast, other homologous proteins such as parvalbumin and the intestinal calcium-binding protein did not bind. Competition studies showed that CaM had a higher affinity for the felodipine-column than sTnC or cTnC. Through studies with a series of proteolytic fragments of CaM and sTnC, it was found that the felodipine binding site is located in the amino-terminal domain of the protein. These results illustrate the utility of affinity-chromatography for the study of dihydropyridine-binding proteins.
DrugBank Data that Cites this Article
- Drug Targets
Drug Target Kind Organism Pharmacological Action Actions Felodipine Calmodulin Protein Humans UnknownOtherDetails Felodipine Troponin C, skeletal muscle Protein Humans UnknownOtherDetails Felodipine Troponin C, slow skeletal and cardiac muscles Protein Humans UnknownOtherDetails