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Study of the Spatial Structure of β-Amyloid Peptide (25-35) from Circular Dichroism Spectroscopy in the Medium Close to Membrane Environment Conditions
Abstract
The spatial structure of β-amyloid peptide (25-35) was studied using circular dichroism spectroscopy in a medium close to the conditions of the membrane environment. The conformational preference of β-amyloid peptide (25-35) was first studied in dipalmitoylphosphatidylcholine (DPPC) solution with and without cholesterol using circular dichroism spectroscopy. It was found that the peptide adopts the structures of the a- helix, β-sheet, β-turn and irregular regions, and their relative proportions changed depending on the presence of cholesterol. The results of the spectral analysis of β-amyloid peptide (25-35) made it possible to unambiguously assume the secondary structure of the peptide in a lipid solvent. It has been shown that ordering of the secondary structure of the β-amyloid peptide (25-35) is observed in the solution with DPPC, which maximally simulates the environment on the surface of the plasma membrane.
About the Authors
G. A. Agaeva
Institute for Physical Problems, Baku State University
Azerbaijan
Azerbaijan
Baku
G. Z. Najafova
French-Azerbaijani University
Azerbaijan
Azerbaijan
Baku
A. Dj. Mammadov
Institute of Biophysics of Ministry of Science and Education of Azerbaijan Republic
Azerbaijan
Azerbaijan
Baku
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Review
For citations:
Agaeva G.A., Najafova G.Z., Mammadov A.D. Study of the Spatial Structure of β-Amyloid Peptide (25-35) from Circular Dichroism Spectroscopy in the Medium Close to Membrane Environment Conditions. Zhurnal Prikladnoii Spektroskopii. 2025;92(2):216-221. (In Russ.)
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