Through space charge transfer (TSCT) based thermally activated delayed fluorescence (TADF) molecules with sky-blue emission have drawn great attentions in recent studies. Corresponding theoretical investigations to reveal the inner mechanisms...

In recent studies, thermally activated delayed fluorescence (TADF) molecules with through space charge transfer (TSCT) feature have aroused wide attentions. Nevertheless, studies about the substitution effects on photophysical properties of...

Conformational changes of membrane proteins are accompanied by deformation in the surrounding lipid bilayer. To gain insight into the energetics of membrane deformation, the phase behavior of dimyristoylphosphatidylcholine (DMPC) membranes in the presence of the dipole potential, ψ d , modifiers was investigated by differential scanning calorimetry. 7-Ketocholesterol, which weakens ψ d and reduces membrane-perpendicular dipole–dipole repulsion, causes a discrete second peak on the high-temperature side of the main transition, whereas 6-ketocholestanol, which strengthens ψ d and increases membrane-perpendicular dipole–dipole repulsion, merely produces a shoulder. Measurements on pure DMPC vesicles showed that the observed temperature profile could not be explained by a single endothermic process, that is, breaking of van der Waals forces between hydrocarbon chains alone. Removal of NaCl from the buffer caused an increase in the main transition temperature and the appearance of an obvious shoulder, implicating polar interactions. Consideration of the phosphatidylcholine (PC) head group dipole moment indicates direct interactions between PC dipoles that are unlikely to account for the additional process. It seems more likely that the breaking of an in-plane hydrogen-bonded network consisting of hydrating water dipoles together with zwitterionic lipid head groups is responsible. The evidence presented supports the idea that the breaking of van der Waals forces between lipid tails required for the main phase transition of PC membranes is coupled to partial breaking of a hydrogen-bonded network at the membrane surface.

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