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The tendency of the A\u03b2(1\u201342) peptide to misfold in solution, correlated to the aetiology of Alzheimer\u2019s disease (AD), is one of the main hindrances to characterising its aggregation kinetics in a cell-mimetic environment. Moreover, the A\u03b2(1\u201342) aggregation triggers the unfolded protein response (UPR) in the endoplasmic reticulum (ER), leading to cellular dysfunction and multiple cell death modalities, exacerbated by reactive oxygen species (ROS), which damage cellular components and trigger inflammation. Antioxidants like curcumin, a derivative of Curcuma longa, help mitigate ER stress by scavenging ROS and enhancing antioxidant enzymes. Furthermore, evidence in the literature highlights the effect of curcumin on the secondary structure of A\u03b2(1\u201342). This explorative study investigates the A\u03b2(1\u201342) peptide conformational behaviour in the presence of curcumin and six derivatives using circular dichroism (CD) to explore their interactions with lipid bilayers, potentially preventing aggregate formation. The results suggest that the synthetic tetrahydrocurcumin (THC) derivative interacts with the amyloid peptide in all the systems presented, while cyclocurcumin (CYC) and bisdemethoxycurcumin (BMDC) only interact when the peptide is in a less stable conformation. Molecular dynamics simulations helped visualise the curcuminoids\u2019 effect in an aqueous system and hypothesise the importance of the peptide surface exposition to the solvent, differently modulated by the curcumin derivatives.<\/jats:p>","DOI":"10.3390\/antiox14010053","type":"journal-article","created":{"date-parts":[[2025,1,6]],"date-time":"2025-01-06T09:17:02Z","timestamp":1736155022000},"page":"53","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":6,"title":["A Structural Effect of the Antioxidant Curcuminoids on the A\u03b2(1\u201342) Amyloid Peptide"],"prefix":"10.3390","volume":"14","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-9690-907X","authenticated-orcid":false,"given":"Angelo","family":"Santoro","sequence":"first","affiliation":[{"name":"Department of Pharmacy, University of Salerno, Via Giovanni Paolo II, 132, 84084 Fisciano, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Antonio","family":"Ricci","sequence":"additional","affiliation":[{"name":"Fresenius Kabi iPSUM, Via San Leonardo, 23, 45010 Villadose, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4412-238X","authenticated-orcid":false,"given":"Manuela","family":"Rodriquez","sequence":"additional","affiliation":[{"name":"Department of Pharmacy, University of Naples Federico II, Via Domenico Montesano, 49, 80131 Naples, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michela","family":"Buonocore","sequence":"additional","affiliation":[{"name":"Department of Pharmacy, University of Salerno, Via Giovanni Paolo II, 132, 84084 Fisciano, Italy"},{"name":"Department of Chemical Sciences and Research Centre on Bioactive Peptides (CIRPEB), University of Naples Federico II, Strada Comunale Cintia, 80126 Naples, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anna Maria","family":"D\u2019Ursi","sequence":"additional","affiliation":[{"name":"Department of Pharmacy, University of Salerno, Via Giovanni Paolo II, 132, 84084 Fisciano, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2025,1,5]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","unstructured":"Serrano-Pozo, A., Frosch, M.P., Masliah, E., and Hyman, B.T. 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