Interfacial Effects on the Conformation of Amyloid-Beta Peptide
Copyright policy )Interfacial Effects on the Conformation of Amyloid-Beta Peptide
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.
- Kansas City University of Medicine and Biosciences United States
Methyl Ethers, Acrylamide, Protein Folding, Amyloid beta-Peptides, Protein Conformation, Surface Properties, Water, Chemical Fractionation, Fluorescence, Peptide Fragments, Sevoflurane, Humans, Tyrosine
Methyl Ethers, Acrylamide, Protein Folding, Amyloid beta-Peptides, Protein Conformation, Surface Properties, Water, Chemical Fractionation, Fluorescence, Peptide Fragments, Sevoflurane, Humans, Tyrosine
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