Inhaled Anesthetics Promote Albumin Dimerization through Reciprocal Exchange of Subdomains

• Main Authors: Benjamin J. Pieters, Eugene E. Fibuch, Joshua D. Eklund, Norbert W. Seidler
• Format: Article
• Language: English
• Published: Hindawi Limited 2010-01-01
• Series: Biochemistry Research International
• Online Access: http://dx.doi.org/10.1155/2010/516704

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