ISSN:
1432-1017
Keywords:
Fluorescent steroid probes
;
steroid-protein interactions, energy alternation of n − π * and π − π * states (level crossing)
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Physics
Notes:
Abstract The physiologically important 3-keto-steroids are non-fluorescent or only weakly fluorescent in protic as well as in aprotic solvents. In contrast, the 4,6,8(14)-triene-3-one steroids are highly fluorescent in aqueous solution but they do not appreciably fluoresce in other solvents. Evidence is presented that the introduction of double bonds into the skeleton of the 3-keto-steroids leads to a decrease of the energy of the lowest π − π * state, bringing this level into the neighbourhood of the non-fluorescent n − π * state. As a consequence, for two states of approximately the same energy, relatively small perturbations such as those due to solvent interactions, protein binding and micelle formation, will then determine whether a system will fluoresce (π − π * state lowest) or not (n − π * state lowest). When the fluorescent 3-keto-steroids, having three conjugated double bonds, bind to proteins, the fluorescence intensity becomes almost zero, making these compounds useful as probes for steroid-protein interactions. This quenching of the fluorescence is explained by a decrease in energy of the n − π * state relative to the π − π * state of the steroids due to hydrophobic interactions with the proteins.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00260400
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