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Электронный каталог: Abdeljawaad, K. A. A. - Temperature-Dependent Conformational Changes of Amyloid-*b42 in DPPC Bilayers
Abdeljawaad, K. A. A. - Temperature-Dependent Conformational Changes of Amyloid-*b42 in DPPC Bilayers
Статья
Автор: Abdeljawaad, K. A. A.
Natural Science Review: Temperature-Dependent Conformational Changes of Amyloid-*b42 in DPPC Bilayers
б.г.
ISBN отсутствует
Автор: Abdeljawaad, K. A. A.
Natural Science Review: Temperature-Dependent Conformational Changes of Amyloid-*b42 in DPPC Bilayers
б.г.
ISBN отсутствует
На полку
Статья
Abdeljawaad, K.A.A.
Temperature-Dependent Conformational Changes of Amyloid-*b42 in DPPC Bilayers / K.A.A.Abdeljawaad, Y.Arynbek, K.Mamatkulov, Huy Le Duc, G.Arzumanyan. – Text : electronic // Natural Science Review. – 2026. – Vol. 3, No. 7. – P. 100704. – URL: https://nsr-jinr.ru/index.php/nsr/article/view/106/97. – Bibliogr.: 68.
The conformational behavior of the amyloid-β42 (Aβ42) peptide is strongly influenced by the physicalstate of its surrounding lipid environment. The effect of temperature on the Aβ42 structure within di-palmitoylphosphatidylcholine (DPPC) bilayers was investigated using circular dichroism (CD), Ramanspectroscopy, 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, rep-resenting the fluid phase above the lipid transition temperature. The CD spectroscopy measurementsindicated a clear temperature-dependent structural transition of the peptide. At RT, Aβ42 exhibited aconformation 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 spec-tral analysis supported this trend by demonstrating an increased contribution of α-helical componentsaccompanied by a reduction in β-strand features upon heating. Minor variations in lipid vibrationalmarkers further suggested greater acyl-chain flexibility and bilayer fluidity in the high-temperaturestate. Furthermore, MD simulations revealed enhanced α-helical content and deeper peptide insertionwithin the disordered bilayer compared with the ordered gel phase. The findings from experimen-tal and computational investigations demonstrate that membrane fluidization above the DPPC phasetransition favors α-helical stabilization of Aβ42, emphasizing temperature as a key parameter govern-ing peptide–lipid conformational equilibria. The results obtained provide a fundamental frameworkfor understanding how thermal conditions modulate amyloid-membrane interactions, which is essentialfor elucidating the early molecular events associated with amyloid-related pathologies.
ОИЯИ = ОИЯИ (JINR)2026
Abdeljawaad, K.A.A.
Temperature-Dependent Conformational Changes of Amyloid-*b42 in DPPC Bilayers / K.A.A.Abdeljawaad, Y.Arynbek, K.Mamatkulov, Huy Le Duc, G.Arzumanyan. – Text : electronic // Natural Science Review. – 2026. – Vol. 3, No. 7. – P. 100704. – URL: https://nsr-jinr.ru/index.php/nsr/article/view/106/97. – Bibliogr.: 68.
The conformational behavior of the amyloid-β42 (Aβ42) peptide is strongly influenced by the physicalstate of its surrounding lipid environment. The effect of temperature on the Aβ42 structure within di-palmitoylphosphatidylcholine (DPPC) bilayers was investigated using circular dichroism (CD), Ramanspectroscopy, 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, rep-resenting the fluid phase above the lipid transition temperature. The CD spectroscopy measurementsindicated a clear temperature-dependent structural transition of the peptide. At RT, Aβ42 exhibited aconformation 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 spec-tral analysis supported this trend by demonstrating an increased contribution of α-helical componentsaccompanied by a reduction in β-strand features upon heating. Minor variations in lipid vibrationalmarkers further suggested greater acyl-chain flexibility and bilayer fluidity in the high-temperaturestate. Furthermore, MD simulations revealed enhanced α-helical content and deeper peptide insertionwithin the disordered bilayer compared with the ordered gel phase. The findings from experimen-tal and computational investigations demonstrate that membrane fluidization above the DPPC phasetransition favors α-helical stabilization of Aβ42, emphasizing temperature as a key parameter govern-ing peptide–lipid conformational equilibria. The results obtained provide a fundamental frameworkfor understanding how thermal conditions modulate amyloid-membrane interactions, which is essentialfor elucidating the early molecular events associated with amyloid-related pathologies.
ОИЯИ = ОИЯИ (JINR)2026
