Interfacial Effects on the Conformation of Amyloid-Beta Peptide

Title: Interfacial Effects on the Conformation of Amyloid-Beta Peptide

Volume: 16 Issue: 2

Author(s): Norbert W. Seidler and Joshua D. Eklund

Affiliation:

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.

Cite this article as:

Seidler W. Norbert and Eklund D. Joshua, Interfacial Effects on the Conformation of Amyloid-Beta Peptide, Protein & Peptide Letters 2009; 16 (2) . https://dx.doi.org/10.2174/092986609787316324