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Article

K16F/E22F Mutation Promotes Oligomerization and Alters β-Sheet Topology of Aβ16-22 Peptides: Insights from Molecular Dynamics Simulations.

ACS chemical neuroscience - 1 Apr 2026

Man Viet Hoang, He Xibing, Niu Taoyu, Cai Lianjin, Han Fengyang, Nguyen Phuong, Wang Junmei

Abstract excerpt

Amyloid-β (Aβ) aggregation into toxic oligomers and fibrils is a hallmark of Alzheimer's disease. The Aβ16-22 fragment plays a critical role in the early stages of the aggregation of full-length Aβ peptides. Aggregation of Aβ16-22 is primarily driven by hydrophobic interactions within the LVFF core and electrostatic attraction between flanking residues K16 (+) and E22 (-). To dissect the relative contributions of...

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Share to Amyloid beta-Peptides
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 41872054
DOI: 10.1021/acschemneuro.6c00003
PMCID: PMC13056258

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