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2000
Volume 16, Issue 2
  • ISSN: 0929-8665
  • E-ISSN: 1875-5305

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.

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/content/journals/ppl/10.2174/092986609787316324
2009-02-01
2025-09-15
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/content/journals/ppl/10.2174/092986609787316324
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  • Article Type:
    Research Article
Keyword(s): Amyloid-beta; fluorescence; interface; protein folding; sevoflurane
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