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The typical symptom of AD is the decline of cognitive abilities, which is caused by loss of synaptic function. Amyloid-\u03b2 (A\u03b2) oligomers play a significant role in the development of this synaptic dysfunction. Neuroligin-(NL)1 is a postsynaptic cell-adhesion molecule located in excitatory synapses and involved in the maintenance and modulation of synaptic contacts. A recent study has found that A\u03b2 interacts with the soluble N-terminal fragment of NL1. The present study aimed to elucidate the role of NL1 in A\u03b2-induced neuropathology. Employing surface plasmon resonance and competitive ELISA, we confirmed the high-affinity binding of NL1 to the A\u03b2 peptide. We also identified a sequence motif representing the NL1-binding site for the A\u03b2 peptide and showed that a synthetic peptide modeled after this motif, termed neurolide, binds to the A\u03b2 peptide with high affinity, comparable to the NL1-A\u03b2 interaction. To assess the effect of neurolide in vivo, wild-type and 5XFAD mice were subcutaneously treated with this peptide for 10\u00a0weeks. We observed an increase in A\u03b2 plaque formation in the cortex of neurolide-treated 5XFAD mice. Furthermore, we showed that neurolide reduces the activity of neprilysin, the predominant A\u03b2-degrading enzyme in the brain. Accordingly, we suggest that neurolide is the NL1-binding site for A\u03b2 peptide, and acts as an inhibitor of neprilysin activity. Based on these data, we confirm the involvement of NL1 in the development of AD and suggest a mechanism for NL1-induced A\u03b2 plaque formation.<\/jats:p>","DOI":"10.1007\/s12035-024-04475-z","type":"journal-article","created":{"date-parts":[[2024,9,11]],"date-time":"2024-09-11T21:02:01Z","timestamp":1726088521000},"page":"3244-3257","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["A Peptide Motif Covering Splice Site B in Neuroligin-1 Binds to A\u03b2 and Acts as a Neprilysin Inhibitor"],"prefix":"10.1007","volume":"62","author":[{"given":"Lene T.","family":"Dietz","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Katrin","family":"P\u00f5ld","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bal\u00e1zs A.","family":"Gy\u00f6rffy","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alexander","family":"Zharkovsky","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jakob B.","family":"S\u00f8rensen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stanislava","family":"Pankratova","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Oksana","family":"Dmytriyeva","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2024,9,11]]},"reference":[{"issue":"s1","key":"4475_CR1","doi-asserted-by":"publisher","first-page":"S567","DOI":"10.3233\/jad-179941","volume":"64","author":"EN Cline","year":"2018","unstructured":"Cline EN, Bicca MA, Viola KL, Klein WL (2018) The amyloid-beta oligomer hypothesis: beginning of the third decade. 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