Электронный каталог

Статья

Abdeljawaad, K.A.A.
pH Modulates Amyloid-*b42 Conformation in Lipid Membranes: Evidence from Circular Dichroism, Raman Spectroscopy, and Molecular Dynamics Simulations / K.A.A.Abdeljawaad, Y.Arynbek, K.Mamatkulov, Hyu Duc Le, M.A.A.Ibrahim, G.F.H.Mekhemer, G.Arzumanyan. – Text : electronic // Journal of Biomolecular Structure and Dynamics. – 2026. – Vol. 44, No. 11. – P. 5189-5204. – URL: https://doi.org/10.1080/07391102.2025.2572296. – Bibliogr.: 70.

Alzheimer’s disease (AD) progression is strongly linked to conformational changes of amyloid-*b42 (A*b42) in neuronal membranes. This study examined the influence of pH on A*b42 conformation in 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) membranes using Raman spectroscopy, circular dichroism (CD), and molecular dynamics (MD) simulations. At acidic pH (5.5), Aβ42 predominantly adopted *a-helical structures (∼75–80%), whereas neutral (pH 7.4) and alkaline conditions (pH 9.5) reduced α-helical content to ∼48–58% and ∼44–47%, respectively, with a corresponding rise in random-coil structures (∼20–36%). Across all pH conditions, *b-sheet content remained minimal, although MD trajectories indicated transient b-bridge contacts suggestive of early aggregation. MD analyses revealed modest pH-dependent perturbations in bilayer thickness and lipid order. Consistency across experimental and computational methods highlights pH as a critical modulator of A*b42 structural dynamics in membranes, providing mechanistic insight into its neurotoxic potential and informing future therapeutic strategies.



Спец.(статьи,препринты) = С 44 б - Разделение химических элементов экстракционными и ионообменными методами
ОИЯИ = ОИЯИ (JINR)2026