{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,21]],"date-time":"2026-08-21T12:12:55Z","timestamp":1787314375570,"version":"build-2736575974"},"reference-count":31,"publisher":"MDPI AG","issue":"15","license":[{"start":{"date-parts":[[2024,7,24]],"date-time":"2024-07-24T00:00:00Z","timestamp":1721779200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Bulgarian National Science Fund","award":["K\u041f-06-KOCT\/8"],"award-info":[{"award-number":["K\u041f-06-KOCT\/8"]}]},{"name":"Bulgarian National Science Fund","award":["Project BG05M2OP001-1.001-0008-C010"],"award-info":[{"award-number":["Project BG05M2OP001-1.001-0008-C010"]}]},{"name":"Centre of Excellence \u2018National center for mechatronics and clean technologies\u2019","award":["K\u041f-06-KOCT\/8"],"award-info":[{"award-number":["K\u041f-06-KOCT\/8"]}]},{"name":"Centre of Excellence \u2018National center for mechatronics and clean technologies\u2019","award":["Project BG05M2OP001-1.001-0008-C010"],"award-info":[{"award-number":["Project BG05M2OP001-1.001-0008-C010"]}]},{"name":"European Regional Development Fund within the Bulgarian OP \u2018Science and Education for Smart Growth 2014\u20132020\u2019","award":["K\u041f-06-KOCT\/8"],"award-info":[{"award-number":["K\u041f-06-KOCT\/8"]}]},{"name":"European Regional Development Fund within the Bulgarian OP \u2018Science and Education for Smart Growth 2014\u20132020\u2019","award":["Project BG05M2OP001-1.001-0008-C010"],"award-info":[{"award-number":["Project BG05M2OP001-1.001-0008-C010"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecules"],"abstract":"<jats:p>The kinetics of amyloid aggregation was studied indirectly by monitoring the changes in the polydispersity of mixed dispersion of amyloid \u03b2 peptide (1-40) and composite liposomes. The liposomes were prepared from the 1,2-dioleoyl-sn-glicero-3-phoshocholine (DOPC) phospholipid and stabilised by the electrostatic adsorption of \u03ba-carrageenan. The produced homotaurine-loaded and unloaded liposomes had a highly negative electrokinetic potential and remarkable stability in phosphate buffer (pH 4 and 7.4). For the first time, the appearance and evolution of the aggregation of A\u03b2 were presented through the variation in the standard percentile readings (D10, D50, and D90) obtained from the particle size distribution analysis. The kinetic experiments indicated the appearance of the first aggregates almost 30 min after mixing the liposomes and peptide solution. It was observed that by adding unloaded liposomes, the size of 90% of the particles in the dispersion (D90) increased. In contrast, the addition of homotaurine-loaded liposomes had almost minimal impact on the size of the fractions of larger particles during the kinetic experiments. Despite the specific bioactivity of homotaurine in the presence of natural cell membranes, this study reported an additional inhibitory effect of the compound on the amyloid peptide aggregation due to the charge effects and \u2018molecular crowding\u2019.<\/jats:p>","DOI":"10.3390\/molecules29153460","type":"journal-article","created":{"date-parts":[[2024,7,24]],"date-time":"2024-07-24T10:46:20Z","timestamp":1721817980000},"page":"3460","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["Investigation of the Aggregation of A\u03b2 Peptide (1-40) in the Presence of \u03ba-Carrageenan-Stabilised Liposomes Loaded with Homotaurine"],"prefix":"10.3390","volume":"29","author":[{"given":"Kamelia","family":"Kamburova","sequence":"first","affiliation":[{"name":"Institute of Physical Chemistry \u2018Acad. R. Kaischew\u2019, Bulgarian Academy of Sciences, 1113 Sofia, Bulgaria"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6343-8670","authenticated-orcid":false,"given":"Ivaylo L.","family":"Dimitrov","sequence":"additional","affiliation":[{"name":"Institute of Physical Chemistry \u2018Acad. R. Kaischew\u2019, Bulgarian Academy of Sciences, 1113 Sofia, Bulgaria"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Feyzim","family":"Hodzhaoglu","sequence":"additional","affiliation":[{"name":"Institute of Physical Chemistry \u2018Acad. R. Kaischew\u2019, Bulgarian Academy of Sciences, 1113 Sofia, Bulgaria"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6737-1936","authenticated-orcid":false,"given":"Viktoria","family":"Milkova","sequence":"additional","affiliation":[{"name":"Institute of Physical Chemistry \u2018Acad. R. Kaischew\u2019, Bulgarian Academy of Sciences, 1113 Sofia, Bulgaria"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2024,7,24]]},"reference":[{"key":"ref_1","unstructured":"(2023, December 08). World Alzheimer Report 2023. Available online: www.alzint.org\/resource\/world-alzheimer-report-2023\/."},{"key":"ref_2","doi-asserted-by":"crossref","unstructured":"Russo, O., Kisialiou, A., Lamonaca, P., Moroni, R., Prinzi, G., and Fimi, M. (2016). New drugs from marine organisms in Alzheimer\u2019s disease. Mar. Drugs, 14.","DOI":"10.3390\/md14010005"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"105208","DOI":"10.1016\/j.neuint.2021.105208","article-title":"Aggregation and structure of amyloid \u03b2-protein","volume":"151","author":"Ono","year":"2021","journal-title":"Neurochem. J."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1016\/j.neuint.2017.08.010","article-title":"Alzheimer\u2019s disease as oligomeropathy","volume":"119","author":"Ono","year":"2018","journal-title":"Neurochem. Int."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"1055","DOI":"10.1016\/0092-8674(93)90635-4","article-title":"Seeding \u2018one-dimensional crystallization\u2019 of amyloid: A pathogenic mechanism in Alzheimer\u2019s disease and scrapie?","volume":"73","author":"Jarrett","year":"1993","journal-title":"Cell"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"2677","DOI":"10.1042\/BCJ20160868","article-title":"The growth of amyloid fibrils; rates and mechanisms","volume":"476","author":"Buell","year":"2019","journal-title":"Biochem. J."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"6288","DOI":"10.1021\/bi992933h","article-title":"Alzheimer\u2019s disease amyloid propagation by a template-dependent dock-lock mechanism","volume":"39","author":"Esler","year":"2000","journal-title":"Biochemistry"},{"key":"ref_8","doi-asserted-by":"crossref","unstructured":"Silva, M., Seijas, P., and Otero, P. (2021). Exploitation of marine molecules to manage Alzheimer\u2019s disease. Mar. Drug, 19.","DOI":"10.3390\/md19070373"},{"key":"ref_9","doi-asserted-by":"crossref","unstructured":"Huang, Y., Chang, Y., Liu, L., and Wang, J. (2021). Nanomaterials for modulating the aggregation of \u03b2-amyloid peptides. Molecules, 26.","DOI":"10.3390\/molecules26144301"},{"key":"ref_10","doi-asserted-by":"crossref","unstructured":"Manzano, S., Ag\u00fcera, L., Aguilar, M., and Olazaran, J.A. (2020). Review on tramiprosate (homotaurine) in Alzheimer\u2019s disease and other neurocognitive disorders. Front. Neurol., 11.","DOI":"10.3389\/fneur.2020.00614"},{"key":"ref_11","doi-asserted-by":"crossref","unstructured":"Kabir, M.T., Sahab Uddin, M., Jeandet, P., Emran, T.B., Mitra, S., Albadrani, G.M., Sayed, A.A., Abdel-Daim, M.M., and Simal-Gandara, J. (2021). Anti-Alzheimer\u2019s molecules derived from marine life: Understanding molecular mechanisms and therapeutic potential. Mar. Drugs, 19.","DOI":"10.3390\/md19050251"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"2510","DOI":"10.3390\/molecules20022510","article-title":"The Effect of Glycosaminoglycans (GAGs) on Amyloid Aggregation and Toxicity","volume":"20","author":"Iannuzzi","year":"2015","journal-title":"Molecules"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"16555","DOI":"10.1038\/s41598-018-32733-3","article-title":"Homotaurine, a safe blood-brain barrier permeable GABAA-R-specific agonist ameliorates diseases in mouse models of multiple sclerosis","volume":"8","author":"Tian","year":"2018","journal-title":"Sci. Rep."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"537","DOI":"10.1016\/j.neurobiolaging.2006.02.015","article-title":"Targeting soluble A\u03b2 peptide with Tramiposate for the treatment of brain amyloidosis","volume":"28","author":"Gervais","year":"2007","journal-title":"Neurobiolol. Aging"},{"key":"ref_15","doi-asserted-by":"crossref","unstructured":"Yao, Z., Jin, L., Li, J., Wang, Y., Lu, R., Bai, Y., and Wu, H. (2022). \u03ba-carrageenan oligosaccharides postpone the progression of Alzheimer\u2019s disease by inhibiting the neuronal damage caused by microglial overactivation. Res. Sq.","DOI":"10.21203\/rs.3.rs-1588494\/v1"},{"key":"ref_16","doi-asserted-by":"crossref","unstructured":"Cao, Y., Dong, X., and Chen, X. (2022). Polymer-modified liposomes for drug delivery: From fundamentals to applications. Pharmaceutics, 14.","DOI":"10.3390\/pharmaceutics14040778"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"19","DOI":"10.56530\/spectroscopy.ua9474q7","article-title":"Spectrophotometric Determination of Thiosulfate in Desulfurization Solutions by Decoloration of Methylene Blue","volume":"38","author":"Zhao","year":"2023","journal-title":"Spectroscopy"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"128141","DOI":"10.1016\/j.chemosphere.2020.128141","article-title":"Effect of acidic conditions on decomposition of methylene blue in aqueous solution by air microbubbles","volume":"263","author":"Minamoto","year":"2021","journal-title":"Chemosphere"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"3362","DOI":"10.1046\/j.1432-1033.2002.03024.x","article-title":"Amyloid-fibril formation. Proposed mechanisms and relevance to conformation disease","volume":"269","author":"Zerovnik","year":"2002","journal-title":"Eur. J. Biochem."},{"key":"ref_20","first-page":"72","article-title":"The role of lipid-protein interactions in amyloid-type protein fibril formation","volume":"141","author":"Gorbenko","year":"2006","journal-title":"Chem. Phys."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"e202210675","DOI":"10.1002\/anie.202210675","article-title":"pH Dependence of Amyloid-\u03b2 Fibril Assembly Kinetics: Unravelling the Microscopic Molecular Processes","volume":"61","author":"Viles","year":"2022","journal-title":"Angew. Chem. Int. Ed."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"266","DOI":"10.1021\/cn400124r","article-title":"Charge Dependent Retardation of Amyloid \u03b2 Aggregation by Hydrophilic Proteins","volume":"5","author":"Assarsson","year":"2014","journal-title":"ACS Chem. Neurosci."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"1175","DOI":"10.1016\/j.jmb.2004.06.086","article-title":"Phospholipid catalysis of diabetic amyloid assembly","volume":"341","author":"Knight","year":"2004","journal-title":"J. Mol. Biol."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1016\/j.bbapap.2003.12.008","article-title":"Conformation constraints for amyloid fibrillation: The importance of being unfolded","volume":"1698","author":"Uversky","year":"2004","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"14851","DOI":"10.1021\/bi9911839","article-title":"Ligand-dependent tau filament formation: Implications for Alzheimer\u2019s disease progression","volume":"38","author":"King","year":"1999","journal-title":"Biochemistry"},{"key":"ref_26","first-page":"2181","article-title":"Free fatty acids simulate the polymerization of tau and amyloid beta peptides. In vitro evidence for a common effector of pathogenesis of Alzheimer\u2019s disease","volume":"150","author":"Wilson","year":"1997","journal-title":"Am. J. Pathol."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1116\/1.3082042","article-title":"Charging and structure of zwitterionic supported bilayer lipid membranes studied by streaming current measurements, fluorescence microscopy, and attenuated total reflection Fourier transform infrared spectroscopy","volume":"4","author":"Zimmermann","year":"2009","journal-title":"Biointerphases"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1016\/j.molstruc.2015.03.023","article-title":"Dependence pH and proposed mechanism for aggregation of Alzheimer\u2019s disease-related amyloid-\u03b2(1\u201342) protein","volume":"1094","author":"Kobayashi","year":"2015","journal-title":"J. Mol. Struct."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"924","DOI":"10.1063\/1.1672157","article-title":"Limiting Laws and Counterion Condensation in Polyelectrolyte Solutions","volume":"51","author":"Manning","year":"1969","journal-title":"J. Chem. Phys."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"3642","DOI":"10.1002\/polb.20206","article-title":"Rod-like Polyelectrolyte Adsorption onto Charged Surfaces in Monovalent and Divalent Salt Solution","volume":"42","author":"Cheng","year":"2004","journal-title":"J. Polym. Sci. Part B Polym. Phys."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"1320","DOI":"10.3390\/neurolint15040083","article-title":"Remdesivir-Loaded Nanoliposomes Stabilized by Chitosan\/Hyaluronic Acid Film with a Potential Application in the Treatment of Coronavirus Infection","volume":"15","author":"Milkova","year":"2023","journal-title":"Neurol Int."}],"container-title":["Molecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1420-3049\/29\/15\/3460\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T15:22:19Z","timestamp":1760109739000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1420-3049\/29\/15\/3460"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,7,24]]},"references-count":31,"journal-issue":{"issue":"15","published-online":{"date-parts":[[2024,8]]}},"alternative-id":["molecules29153460"],"URL":"https:\/\/doi.org\/10.3390\/molecules29153460","relation":{},"ISSN":["1420-3049"],"issn-type":[{"value":"1420-3049","type":"electronic"}],"subject":[],"published":{"date-parts":[[2024,7,24]]}}}