The effect of binding of chlorpromazine and chloroquine to ion transporting ATPases.
The inhibition of ion transporting ATPases (Na+,K+-ATPase, Ca2+,Mg2+- and Ca2+-ATPase) by two amphiphilic drugs e.g. chlorpromazine (antipsychotic) and chloroquine (antimalarial) are found to be competitive in nature in vitro with respect to the substrate. Two binding sites - high and low affinity are found to exist on all the three ATPases toward these drugs as evident from the plot of F/F0 vs. different drug concentrations of tryptophan fluorescence of the enzymes. Circular dichroism analysis suggest that binding of drugs to the high affinity site does not involve any change in conformation of ATPase molecules which occur only when drug binds to the low affinity sites. The drug binding sites and possible effect on conformational change of ATPase molecules of these two drugs have been described in this report.
Bhattacharyya
D
D
Department of Chemistry, Bose Institute, Calcutta, India.
Sen
P C
PC
D000251:Adenosine Triphosphatases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D000818:Animals; D001921:Brain / Q000201:enzymology; D002738:Chloroquine / Q000378:metabolism*; D002746:Chlorpromazine / Q000378:metabolism*; D002942:Circular Dichroism; D005453:Fluorescence; D008297:Male; D011485:Protein Binding; D051381:Rats
D002738:Chloroquine; D000251:Adenosine Triphosphatases; D002746:Chlorpromazine