Title: Interfacial Effects on the Conformation of Amyloid-Beta Peptide
VOLUME: 16 ISSUE: 2
Author(s):Norbert W. Seidler and Joshua D. Eklund
Affiliation:Department of Biochemistry, Kansas City University of Medicine and Biosciences, 1750 Independence Avenue, Kansas City, Missouri 64106, USA.
Keywords:Amyloid-beta, interface, sevoflurane, fluorescence, protein folding
Abstract: We examined the effects of air-water and water-sevoflurane interfaces on conformational properties of amyloid- β peptide (ABP). Fractions were extracted from sub-interfacial (air-water) and supra-interfacial (water-sevoflurane) layers and compared with aqueous bulk layers using fluorescence properties of ABP provided by a single tyrosine. The observations suggest that interfacial ABP may be more disordered than bulk ABP.
