Document Type
Article
Publication Title
Biochemistry Research International
Abstract
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.
DOI
10.1155/2010/516704
Publication Date
3-24-2010
ISSN
2090-2255
Recommended Citation
Pieters BJ, Fibuch EE, Eklund JD, Seidler NW. Inhaled Anesthetics Promote Albumin Dimerization through Reciprocal Exchange of Subdomains. Biochemistry Research International. 2010; 2010. doi: 10.1155/2010/516704.
