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Imipramine binds to Amyloid-beta(1-42) monomers in vitro, as shown by NMR spectroscopy.

Beham, J.; Johnson, N. R.; Vögeli, B.; Henen, M. A.; Vugmeyster, L.

2026-08-27 biophysics
10.64898/2026.08.24.746779 bioRxiv
Show abstract

Imipramine is known as an older generation tricyclic antidepressant drug. It has been identified in prior studies that imipramine blocks Apolipoprotein E4 (ApoE4)-induced amyloid-{beta}(A{beta}) aggregation and is associated with an improved AD diagnosis [Johnson et al. Alzheimers Research Therapy, 2022, 14, 88]. Using NMR methods such as 1H-1H NOESY and Saturation Transfer Difference Spectroscopy, we demonstrate the binding of A{beta} monomers to imipramine when the full-length A{beta} (1-42) sequence is considered. The more abundant but less toxic form, A{beta} (1-40) does not show interaction with imipramine.

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