Inhaled Anesthetics Promote Albumin Dimerization through Reciprocal Exchange of Subdomains.

摘要: Inhaled anesthetics affect protein-protein interaction, but the mechanisms underlying these effects are still poorly understood. We examined impact of sevoflurane and isoflurane on dimerization human serum albumin (HSA), a protein with anesthetic binding sites that well characterized. Intrinsic fluorescence emission was analyzed for spectral shifting self-quenching, control first derivatives (spectral responses to changes in HSA concentration) were compared against those obtained from samples treated or isoflurane. Sevoflurane increased dimer-dependent self-quenching both decreased oligomer-dependent shifting, suggesting inhaled promoted dimerization. Size exclusion chromatography polarization data consistent observations. The support proposed model reciprocal exchange subdomains form an dimer. open-ended subdomains, which we propose occuring oligomers, inhibited by