Equilibrium binding constants for Tl+ with gramicidins A, B and C in a lysophosphatidylcholine environment determined by 205Tl nuclear magnetic resonance spectroscopy.
| Publication Type | Academic Article |
| Authors | Hinton J, Koeppe R, Shungu D, Whaley W, Paczkowski J, Millett F |
| Journal | Biophys J |
| Volume | 49 |
| Issue | 2 |
| Pagination | 571-7 |
| Date Published | 02/01/1986 |
| ISSN | 0006-3495 |
| Keywords | Gramicidin, Lysophosphatidylcholines, Thallium |
| Abstract | Nuclear Magnetic Resonance (NMR) 205Tl spectroscopy has been used to monitor the binding of Tl+ to gramicidins A, B, and C packaged in aqueous dispersions of lysophosphatidylcholine. For 5 mM gramicidin dimer in the presence of 100 mM lysophosphatidylcholine, only approximately 50% or less of the gramicidin appears to be accessible to Tl+. Analysis of the 205Tl chemical shift as a function of Tl+ concentration over the 0.65-50 mM range indicates that only one Tl+ ion can be bound by gramicidin A, B, or C under these experimental conditions. In this system, the Tl+ equilibrium binding constant is 582 +/- 20 M-1 for gramicidin 1949 +/- 100 M-1 for gramicidin B, and 390 +/- 20 M-1 for gramicidin C. Gramicidin B not only binds Tl+ more strongly but it is also in a different conformational state than that of A and C, as shown by Circular Dichroism spectroscopy. The 205Tl NMR technique can now be extended to determinations of binding constants of other cations to gramicidin by competition studies using a 205Tl probe. |
| DOI | 10.1016/S0006-3495(86)83668-2 |
| PubMed ID | 2420383 |
| PubMed Central ID | PMC1329498 |