Topic: amyloid beta peptide

Recent studies have highlighted the dual role of amyloid beta peptide (Aβ) in both Alzheimer’s disease (AD) and normal brain function. Particularly, Αβ1-40 and Αβ1-42 are key in regulating homeostatic synaptic plasticity in the dentate gyrus. This study aimed to identify specific amyloid fragments (N- and C- terminus fragments of Αβ) involved in synaptic plasticity modulation. Using entorhino-hippocampal tissue cultures, combined with whole-cell patch clamp recordings, light- and electron microscopy and molecular biology techniques, we found that the N-terminal fragment Aβ1-16 is essential for

Dysfunctional α7 nicotinic acetylcholine receptors (α7*nAChRs) and their genetic regulation have been associated with several neuropsychiatric diseases, including schizophrenia and Alzheimer’s disease (AD). Preclinical studies revealed that α7*nAChR ligands can improve executive function, commonly impaired across neuropsychiatric disorders. Yet, a translational gap prevents these findings from resulting into clinically effective treatments. To tackle this translational gap, we combine approaches such as transgenic rats, viral vector-mediated local gene expression, touchscreen-based behavioral