Interfacial Effects on the Conformation of Amyloid-Beta Peptide
Document Type
Article
Publication Title
Protein and Peptide Letters
Abstract
We examined the effects of air-water and water-sevoflurane interfaces on conformational properties of amyloid-beta 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.
DOI
10.2174/092986609787316324
Publication Date
2-2009
Keywords
Amyloid-beta, interface, sevoflurane, fluorescence, protein folding
ISSN
1875-5305
Recommended Citation
Seidler NW, Eklund JD. Interfacial Effects on the Conformation of Amyloid-Beta Peptide. Protein and Peptide Letters. 2009; 16(2). doi: 10.2174/092986609787316324.
