Thermodynamic parameters for the binding of divalent cations to gramicidin A incorporated into a lipid environment by Tl-205 nuclear magnetic resonance.
Thermodynamic parameters, enthalpy and entropy, for the binding of the divalent cations, Mg+2, Ca+2, Sr+2, Ba+2, and Cd+2, to gramicidin A, incorporated into lysophosphatidylcholine, have been determined using a combination of Tl-205 nuclear magnetic resonance spectroscopy and competition binding. The binding process is thermodynamically driven by the enthalpy and not the entropy. The enthalpy values are related to the process involving the transfer of cations from an aqueous environment to an amide environment. A comparison is made between the thermodynamic parameters for the binding of monovalent and divalent cations to gramicidin A to illustrate the channel blocking ability of the divalent cations with respect to monovalent cation transport.
Hinton
J F
JF
Department of Chemistry and Biochemistry, University of Arkansas, Fayetteville 72701.
Fernandez
J Q
JQ
Shungu
D C
DC
Millett
F S
FS
D002412:Cations; D006096:Gramicidin; D008051:Lipid Bilayers; D008244:Lysophosphatidylcholines; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008954:Models, Biological; D011485:Protein Binding; D013816:Thermodynamics
D002412:Cations; D008051:Lipid Bilayers; D008244:Lysophosphatidylcholines; D006096:Gramicidin