Amyloid-beta-sheet formation at the air-water interface.
An amyloid(1-40) solution rich in coil, turn, and alpha-helix, but poor in beta-sheet, develops monolayers with a high beta-sheet content when spread at the air-water interface. These monolayers are resistant to repeated compression-dilatation cycles and interaction with trifluoroethanol. The secondary structure motifs were detected by circular dichroism (CD) in solution and with infrared reflection-absorption spectroscopy (IRRAS) at the interface. Hydrophobic influences are discussed for the structure conversion in an effort to understand the completely unknown reason for the natural change of the normal prion protein cellular (PrP(C)) into the abnormal prion protein scrapie (PrP(Sc)).
Schladitz
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Max-Planck-Institute for Colloids and Interfaces, Campus Golm, D-14476 Potsdam, Germany.
Vieira
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Hermel
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Möhwald
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D000388:Air; D000595:Amino Acid Sequence; D000682:Amyloid / Q000737:chemistry*; D000818:Animals; D055592:Biophysical Phenomena; D001703:Biophysics; D002942:Circular Dichroism; D006801:Humans; D066298:In Vitro Techniques; D008958:Models, Molecular; D008969:Molecular Sequence Data; D018621:PrPC Proteins / Q000737:chemistry; D018620:PrPSc Proteins / Q000737:chemistry; D017433:Protein Structure, Secondary; D013055:Spectrophotometry, Infrared; D014867:Water
D000682:Amyloid; D018621:PrPC Proteins; D018620:PrPSc Proteins; D014867:Water