Inhaled Anesthetics Promote Albumin Dimerization through Reciprocal Exchange of Subdomains

• Published in: Biochemistry Research International Vol. 2010; no. 2010; pp. 1 - 7
• Main Authors: Pieters, Benjamin J., Fibuch, Eugene E., Eklund, Joshua D., Seidler, Norbert W.
• Format: Journal Article
• Language: English
• Published: Cairo, Egypt Hindawi Limiteds 01.01.2010; Hindawi Puplishing Corporation; Hindawi Publishing Corporation; Wiley
• ISSN: 2090-2247; 2090-2255
• DOI: 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.