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.
Seidler
Norbert W
NW
Department of Biochemistry, Kansas City University of Medicine and Biosciences, 1750 Independence Avenue, Kansas City, Missouri 64106 USA. nseidler@kcumb.edu.
Eklund
Joshua D
JD
D020106:Acrylamide / Q000737:chemistry; D016229:Amyloid beta-Peptides / Q000737:chemistry* / Q000378:metabolism; D005591:Chemical Fractionation; D005453:Fluorescence; D006801:Humans; D008738:Methyl Ethers / Q000737:chemistry; D010446:Peptide Fragments / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D017510:Protein Folding; D000077149:Sevoflurane; D013499:Surface Properties; D014443:Tyrosine / Q000737:chemistry; D014867:Water / Q000737:chemistry
D016229:Amyloid beta-Peptides; D008738:Methyl Ethers; D010446:Peptide Fragments; C075222:amyloid beta-protein (1-42); D014867:Water; D020106:Acrylamide; D000077149:Sevoflurane; D014443:Tyrosine