{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Consoli GML"],"funding":["European Social Fund","Dipartimento regionale dell?Istruzione e della Formazione Professionale","Regione Siciliana","Avviso pubblico"],"pagination":["1449-1462"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9535895"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["12(8)"],"pubmed_abstract":["Alzheimer's disease (AD) is a progressive neurodegenerative condition affecting people in the elderly. Targeting aggregation of β-amyloid peptides (Aβ) is considered a promising approach for the therapeutic treatment of the disease. Peptide based inhibitors of β-amyloid fibrillation are emerging as safe drug candidates as well as interesting compounds for early diagnosis of AD. Peptide conjugation via covalent bond with functional moieties enables the resultant hybrid system to acquire desired functions. Here we report the synthesis, the structural characterization, and the Aβ<sub>42</sub> interaction of a <i>p</i>-amino-calix[4]arene derivative bearing a GPGKLVFF peptide pendant at the lower rim. We demonstrate that the <i>p</i>-amino-calix[4]arene-GPGKLVFF conjugate alters the Aβ<sub>42<"],"journal":["ACS chemical neuroscience"],"pubmed_title":["Novel Peptide-Calix[4]arene Conjugate Inhibits Aβ Aggregation and Rescues Neurons from Aβ's Oligomers Cytotoxicity <i>In Vitro</i>."],"pmcid":["PMC9535895"],"funding_grant_id":["N.11/2017"],"pubmed_authors":["Baglieri A","Petralia S","Pappalardo G","Tosto R","Giuffrida ML","Consoli GML","Zimbone S","Campagna T","Di Natale G"],"additional_accession":[]},"is_claimable":false,"name":"Novel Peptide-Calix[4]arene Conjugate Inhibits Aβ Aggregation and Rescues Neurons from Aβ's Oligomers Cytotoxicity <i>In Vitro</i>.","description":"Alzheimer's disease (AD) is a progressive neurodegenerative condition affecting people in the elderly. Targeting aggregation of β-amyloid peptides (Aβ) is considered a promising approach for the therapeutic treatment of the disease. Peptide based inhibitors of β-amyloid fibrillation are emerging as safe drug candidates as well as interesting compounds for early diagnosis of AD. Peptide conjugation via covalent bond with functional moieties enables the resultant hybrid system to acquire desired functions. Here we report the synthesis, the structural characterization, and the Aβ<sub>42</sub> interaction of a <i>p</i>-amino-calix[4]arene derivative bearing a GPGKLVFF peptide pendant at the lower rim. We demonstrate that the <i>p</i>-amino-calix[4]arene-GPGKLVFF conjugate alters the Aβ<sub>42<","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Apr","modification":"2025-04-26T22:08:29.334Z","creation":"2025-02-19T00:27:19.862Z"},"accession":"S-EPMC9535895","cross_references":{"pubmed":["33844495"],"doi":["10.1021/acschemneuro.1c00117"]}}