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Structure dependent effects of Amyloid-ß on long-term memory in Lymnaea stagnalis

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Version 2 2023-06-12, 08:40
Version 1 2023-06-09, 05:37
journal contribution
posted on 2023-06-12, 08:40 authored by Lenzie Ford, Michael CrossleyMichael Crossley, Devkee M Vadukul, György Kemenes, Louise SerpellLouise Serpell
Amyloid-ß (Aß) peptides are implicated in the causation of memory loss, neuronal impairment, and neurodegeneration in Alzheimer's disease. Our recent work revealed that Aß 1–42 and Aß 25–35 inhibit long-term memory (LTM) recall in Lymnaea stagnalis (pond snail) in the absence of cell death. Here, we report the characterization of the active species prepared under different conditions, describe which Aß species is present in brain tissue during the behavioral recall time point and relate the sequence and structure of the oligomeric species to the resulting neuronal properties and effect on LTM. Our results suggest that oligomers are the key toxic Aß1–42 structures, which likely affect LTM through synaptic plasticity pathways, and that Aß 1–42 and Aß 25–35 cannot be used as interchangeable peptides.

History

Publication status

  • Published

File Version

  • Published version

Journal

FEBS Letters

ISSN

0014-5793

Publisher

Elsevier

Issue

9

Volume

591

Page range

1236-1246

Department affiliated with

  • Biochemistry Publications

Research groups affiliated with

  • Dementia Research Group Publications

Full text available

  • Yes

Peer reviewed?

  • Yes

Legacy Posted Date

2017-04-04

First Open Access (FOA) Date

2017-04-04

First Compliant Deposit (FCD) Date

2017-04-04

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