Herpes Simplex Virus Glycoprotein D Associated with Aβ1–42 Tetramers Mediates Neurotoxicity by Perturbing Neuronal Membrane Integrity: A Molecular Dynamics Simulation

Alzheimer’s disease (AD) is characterized by deleterious amyloid plaques deposited in the brain, formed through the interaction of Amyloid β-peptides (Aβ1–42) with the cell membrane. Despite promising preclinical results, Aβ1–42 aggregation inhibitors ha...

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Bibliographic Details
Main Author:	Subramanian Boopathi (8733639) (author)
Other Authors:	Ramón Garduño-Juárez (10702425) (author), M. Michael Gromiha (7390772) (author)
Published:	2025
Subjects:	Biophysics Biochemistry Medicine Cell Biology Molecular Biology Neuroscience Pharmacology Cancer Infectious Diseases Computational Biology Chemical Sciences not elsewhere classified study provides atomic may significantly contribute discrepancy may stem demonstrates significant adsorption atom molecular dynamics mounting evidence suggests tetramers mediates neurotoxicity neurotoxicity remains elusive robust electrostatic interactions neuronal cell loss interaction significantly reduces 1 envelope glycoprotein – membrane interactions lipid membrane integrity molecular mechanism underlying – gd binding gd amplifies aβ – gd cell membrane underlying mechanism neuronal membranes lipid bilayers level evidence gd protein thoroughly investigate thereby suggesting pronounced upon phosphate groups performed extensive initial stages demanding task clinical trials charged residues binding alone aqueous environments anticipated benefits amyloid β 1 infection
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Herpes Simplex Virus Glycoprotein D Associated with Aβ<sub>1–42</sub> Tetramers Mediates Neurotoxicity by Perturbing Neuronal Membrane Integrity: A Molecular Dynamics Simulation

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