Abstract
The NMR analysis of fluorine-containing molecules, increasingly widespread due to their importance in pharmaceuticals and biochemistry, poses significant
challenges. Severe peak overlap in the proton spectrum often hinders the extraction of critical structural information in the form of heteronuclear scalar coupling constants, crucial for determining pharmaceutical properties and biological activity. Here, a new method, IPAP-FESTA, is reported that drastically simplifies measurements of the signs and magnitudes of proton-fluorine couplings. Its usefulness is demonstrated for the structural study of the steroidal drug fluticasone
propionate extracted from a commercial formulation, and for assessing solvent effects on the conformational equilibrium in a physically inseparable fluorohydrin mixture.
challenges. Severe peak overlap in the proton spectrum often hinders the extraction of critical structural information in the form of heteronuclear scalar coupling constants, crucial for determining pharmaceutical properties and biological activity. Here, a new method, IPAP-FESTA, is reported that drastically simplifies measurements of the signs and magnitudes of proton-fluorine couplings. Its usefulness is demonstrated for the structural study of the steroidal drug fluticasone
propionate extracted from a commercial formulation, and for assessing solvent effects on the conformational equilibrium in a physically inseparable fluorohydrin mixture.
| Original language | English |
|---|---|
| Journal | Journal of the American Chemical Society |
| Publication status | Accepted/In press - 9 Aug 2023 |