{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,18]],"date-time":"2026-08-18T13:59:02Z","timestamp":1787061542595,"version":"build-2736575974"},"reference-count":65,"publisher":"Wiley","issue":"19","license":[{"start":{"date-parts":[[2023,8,10]],"date-time":"2023-08-10T00:00:00Z","timestamp":1691625600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["chemistry-europe.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["ChemBioChem"],"published-print":{"date-parts":[[2023,10,4]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    Cyclodextrins are saccharide ring\u2009molecules which act as host cavities that can encapsulate small guest molecules or thread polymer chains. We investigate the influence of alpha\u2010cyclodextrin (\u03b1CD) on the aqueous solution self\u2010assembly of a peptide\u2010polymer conjugate YYKLVFF\u2010PEG3K previously studied by our group [Castelletto\n                    <jats:italic>et\u2005al<\/jats:italic>\n                    .,\n                    <jats:italic>Polym. Chem<\/jats:italic>\n                    ., 2010, 1, 453\u2013459]. This conjugate comprises a designed amyloid\u2010forming peptide YYKLVFF that contains the KLVFF sequence from Amyloid \u03b2 peptide, A\u03b216\u201020, along with two aromatic tyrosine residues to enhance hydrophobicity, as well as polyethylene glycol PEG with molar mass 3\u2005kg\u2009mol\n                    <jats:sup>\u22121<\/jats:sup>\n                    . The conjugate self\u2010assembles into \u03b2\u2010sheet fibrils in aqueous solution. Here we show that complexation with \u03b1CD instead generates free\u2010floating nanosheets in aqueous solution (with a \u03b2\u2010sheet structure). The nanosheets comprise a bilayer with a hydrophobic peptide core and highly swollen PEG outer layers. The transition from fibrils to nanosheets is driven by an increase in the number of \u03b1CD molecules threaded on the PEG chains, as determined by\n                    <jats:sup>1<\/jats:sup>\n                    H NMR spectroscopy. These findings point to the use of cyclodextrin additives as a powerful means to tune the solution self\u2010assembly in peptide\u2010polymer conjugates and potentially other polymer\/biomolecular hybrids.\n                  <\/jats:p>","DOI":"10.1002\/cbic.202300472","type":"journal-article","created":{"date-parts":[[2023,8,2]],"date-time":"2023-08-02T04:07:13Z","timestamp":1690949233000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":5,"title":["Tuning the Solution Self\u2010Assembly of a Peptide\u2010PEG (Polyethylene Glycol) Conjugate with \u03b1\u2010Cyclodextrin"],"prefix":"10.1002","volume":"24","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-3705-0162","authenticated-orcid":false,"given":"Valeria","family":"Castelletto","sequence":"first","affiliation":[{"name":"School of Chemistry Food Biosciences and Pharmacy University of Reading  Whiteknights Reading RG6 6AD UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Radoslaw M.","family":"Kowalczyk","sequence":"additional","affiliation":[{"name":"School of Chemistry Food Biosciences and Pharmacy University of Reading  Whiteknights Reading RG6 6AD UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jani","family":"Seitsonen","sequence":"additional","affiliation":[{"name":"Nanomicroscopy Center Aalto University  Puumiehenkuja 2 02150 Espoo Finland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4549-0926","authenticated-orcid":false,"given":"Ian W","family":"Hamley","sequence":"additional","affiliation":[{"name":"School of Chemistry Food Biosciences and Pharmacy University of Reading  Whiteknights Reading RG6 6AD UK"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2023,8,10]]},"reference":[{"key":"e_1_2_9_1_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.1205962"},{"key":"e_1_2_9_2_1","doi-asserted-by":"publisher","DOI":"10.1021\/cr970027"},{"key":"e_1_2_9_3_1","unstructured":"\u00a0"},{"key":"e_1_2_9_4_2","doi-asserted-by":"publisher","DOI":"10.1021\/js950534b"},{"key":"e_1_2_9_5_2","doi-asserted-by":"publisher","DOI":"10.1021\/cr970025p"},{"key":"e_1_2_9_6_2","doi-asserted-by":"publisher","DOI":"10.1038\/nrd1576"},{"key":"e_1_2_9_7_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0032-9592(03)00258-9"},{"key":"e_1_2_9_8_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.addr.2007.05.012"},{"key":"e_1_2_9_9_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.ijpharm.2006.10.044"},{"key":"e_1_2_9_10_1","unstructured":"J. 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