Temperature-dependent conformational changes of amyloid-β42 in DPPC bilayers
Температурно-зависимые конформационные изменения бета-амилоида 42 в билипидных слоях DPPC

Additional data

Submitted: 05.03.2026; Accepted: 01.06.2026; Published 25.06.2026;
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How to Cite

K. A. A. Abdeljawaad, Y. Arynbek, K. Mamatkulov, Huy Le Duc, G. Arzumanyan "Temperature-dependent conformational changes of amyloid-β42 in DPPC bilayers" Natural Sci. Rev. 3 100704 (2026)
https://doi.org/10.54546/NaturalSciRev.100704
BibTex
K. A. A. Abdeljawaad1,2,3,a, Y. Arynbek1,4,5, K. Mamatkulov1, Huy Le Duc1,6,7, G. Arzumanyan1
  • 1Joint Institute for Nuclear Research, Dubna, Russia
  • 2Academy of Scientific Research & Technology (ASRT), Cairo, Egypt
  • 3Chemistry Department, Faculty of Science, Minia University, Minia, Egypt
  • 4Faculty of Physics and Technology, al-Farabi Kazakh National University, Almaty, Kazakhstan
  • 5Institute of Nuclear Physics, Almaty, Kazakhstan
  • 6Institute of Physics, Vietnam Academy of Science and Technology, Hanoi, Vietnam
  • 7Graduate University of Science and Technology, Vietnam Academy of Science and Technology, Hanoi, Vietnam
  • akhlood@jinr.ru
DOI: 10.54546/NaturalSciRev.100704
Keywords: Amyloid-β42, Raman spectroscopy, circular dichroism, DPPC, molecular dynamics simulation
Topics: Physics , Condensed Matter Physics (Experiment)
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Abstract

The conformational behavior of the amyloid-β42 (Aβ42) peptide is strongly influenced by the physical state of its surrounding lipid environment. The effect of temperature on the Aβ42 structure within dipalmitoylphosphatidylcholine (DPPC) bilayers was investigated using circular dichroism (CD), Raman spectroscopy, and molecular dynamics (MD) simulations. The study examined two thermal phases: room temperature (RT =∼ (25±2)◦C), corresponding to the gel phase of DPPC, and (48±2)◦C, representing the fluid phase above the lipid transition temperature. The CD spectroscopy measurements indicated a clear temperature-dependent structural transition of the peptide. At RT, Aβ42 exhibited a conformation enriched in β structures, while at (48±2)◦C, the spectra revealed a notable increase in α-helical content, reflecting enhanced backbone organization under fluid-phase conditions. Raman spectral analysis supported this trend by demonstrating an increased contribution of α-helical components accompanied by a reduction in β-strand features upon heating. Minor variations in lipid vibrational markers further suggested greater acyl-chain flexibility and bilayer fluidity in the high-temperature state. Furthermore, MD simulations revealed enhanced α-helical content and deeper peptide insertion within the disordered bilayer compared with the ordered gel phase. The findings from experimental and computational investigations demonstrate that membrane fluidization above the DPPC phase transition favors α-helical stabilization of Aβ42, emphasizing temperature as a key parameter governing peptide–lipid conformational equilibria. The results obtained provide a fundamental framework for understanding how thermal conditions modulate amyloid-membrane interactions, which is essential for elucidating the early molecular events associated with amyloid-related pathologies.

Acknowledgements

The authors have benefited from useful access to the Hybrilit heterogeneous computing platform, which was kindly provided by MLIT JINR.

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