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Journal Article

Selective ion binding and membrane activity of synthetic cyclopeptides


Grell,  Ernst
Molecular Biophysics Group, Max Planck Institute of Biophysics, Max Planck Society;

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Gisin, B., Ting-Beall, H., Davis, D., Grell, E., & Tosteson, D. (1978). Selective ion binding and membrane activity of synthetic cyclopeptides. Biochimica et Biophysica Acta-Biomembranes, 509(2), 201-217. doi:10.1016/0005-2736(78)90041-x.

Cite as: https://hdl.handle.net/21.11116/0000-0008-CA83-0
Four cyclic peptides related to the membrane-active complexones PV, cyclo-(l-Pro-l-Val-d-Pro-d-Val)3, and valinomycin were synthesized: (1) cyclo-(l-Pro-l-Ala-d-Pro-d-Val)3 or PVPA, (2) cyclo-(l-Ala-l-Val-d-Pro-d-Val)3 or PVAV, (3) cyclo-(l-Pro-l-Val-d-Pro-d-Val)2-l-Pro-d-Val or PV-10, (4) cyclo-(l-Pro-l-Val-d-Pro-d-Val)2 or PV-8. In a two-phase extraction assay the affinity of PV and PVPA for alkali picrates was about three orders or magnitude greater than that of valinomycin. It was about equal to valinomycin for PVAV and much lower for PV-10 and PV-8. PV, PVPA and PVAV showed a selectivity sequence similar to that of valinomycin, namely K+ ∼ Rb+ > Cs+ > Na+ > Li+. In the series PV, PV-10, PV-8 the preference for K+ over Na+ was 700, 5 and <1, respectively. Thus, it was possible to reverse the selectivity of PV for K+ over Na+ by reducing the ring size from 12 to 8 amino acid residues.
In sheep red cell lipid bilayer membranes PVPA increased the membrane conductance significantly in the presence of either KCl or NaCl but it was less potent than PV. PV-10, PV-8 and PVAV on the other hand were ineffective in this assay. The inactivity of PVAV as a potassium carrier in membranes was in contrast to its high affinity for potassium picrate in two-phase assays. Such a behaviour may be observed of a compound that has too low an aqueous cation binding constant to use the solution-complexation mechanism of PV (Davis et al. (1976) Biochemistry 15, 768–774 and Pinkerton et al. (1969) Biochem. Biophys. Res. Commun. 35, 512–518) and too slow binding and release kinetics to use the interfacial-complexation mechanism of valinomycin.