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<p>The spatial structure of β-amyloid peptide (25-35) was studied using circular dichroism spectroscopy in a medium with conditions similar to the membrane environment. The conformation preference of β-amyloid peptide (25-35) was first studied in dipalmitoylphosphatidylcholine (DPPC) solution with and without cholesterol using circular dichroism spectroscopy. This peptide was found to adopt α-helix, β-sheet, and β-turn structures along with having irregular regions. The relative proportions of these structural segments were found to depend on the presence of cholesterol. The results of the spectral analysis of β-amyloid peptide (20-35) suggested the secondary structure of this peptide in a lipid solvent. Ordering of the secondary structure of β-amyloid peptide (20-35) was found in the DPPC solution, which has conditions most similar to the environment of the plasma membrane surface.</p>

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Circular Dichroism Spectroscopy Study of the Spatial Structure of β-amyloid Peptide (25-35) in a Medium with Conditions Similar to the Membrane Environment

  • 期刊论文

  • 发表日期：

    2025年5月29日

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  • G. A. Agaeva,
  • G. Z. Najafova,
  • A. Dj. Mammadova

摘要

The spatial structure of β-amyloid peptide (25-35) was studied using circular dichroism spectroscopy in a medium with conditions similar to the membrane environment. The conformation preference of β-amyloid peptide (25-35) was first studied in dipalmitoylphosphatidylcholine (DPPC) solution with and without cholesterol using circular dichroism spectroscopy. This peptide was found to adopt α-helix, β-sheet, and β-turn structures along with having irregular regions. The relative proportions of these structural segments were found to depend on the presence of cholesterol. The results of the spectral analysis of β-amyloid peptide (20-35) suggested the secondary structure of this peptide in a lipid solvent. Ordering of the secondary structure of β-amyloid peptide (20-35) was found in the DPPC solution, which has conditions most similar to the environment of the plasma membrane surface.