{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,8]],"date-time":"2026-07-08T14:49:07Z","timestamp":1783522147951,"version":"3.55.0"},"reference-count":75,"publisher":"MDPI AG","issue":"3","license":[{"start":{"date-parts":[[2025,2,6]],"date-time":"2025-02-06T00:00:00Z","timestamp":1738800000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Australian Government"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Disrupted clearance of amyloid beta (A\u03b2) from the brain enhances its aggregation and formation of amyloid plaques in Alzheimer\u2019s disease. The most abundant protein constituent of circulating high-density lipoprotein (HDL) particles, apoA-I, readily crosses the blood\u2013brain barrier from periphery circulation, exhibits low-micromolar binding affinity for soluble, neurotoxic forms of A\u03b2, and modulates A\u03b2 aggregation and toxicity in vitro. Its highly conserved N-terminal sequence, 42LNLKLLD48 (\u2018LN\u2019), has been proposed as a binding region for A\u03b2. However, high-resolution structural characterisation of the mechanism of HDL\u2013A\u03b2 interaction is very difficult to attain. Molecular dynamics simulations were conducted to investigate for the first time the interaction of A\u03b2 and the \u2018LN\u2019 segment of apoA-I. Favourable binding of A\u03b2 by HDLs was found to be driven by hydrophobic and hydrogen-bonding interactions predominantly between the \u2018LN\u2019 segment of apoA-I and A\u03b2. Preferential binding of A\u03b2 may proceed in small, protein-rich HDLs whereby solvent-exposed hydrophobic \u2018LN\u2019 segments of apoA-I interact specifically with A\u03b2, stabilising it on the HDL surface in a possibly non-amyloidogenic conformation, facilitating effective A\u03b2 clearance. These findings rationalise the potentially therapeutic role of HDLs in reducing A\u03b2 aggregation and toxicity, and of peptide mimics of the apoA-I interacting region in blocking A\u03b2 aggregation.<\/jats:p>","DOI":"10.3390\/ijms26031380","type":"journal-article","created":{"date-parts":[[2025,2,6]],"date-time":"2025-02-06T08:53:41Z","timestamp":1738832021000},"page":"1380","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":7,"title":["Molecular Simulation of the Binding of Amyloid Beta to Apolipoprotein A-I in High-Density Lipoproteins"],"prefix":"10.3390","volume":"26","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-8865-090X","authenticated-orcid":false,"given":"Chris J.","family":"Malajczuk","sequence":"first","affiliation":[{"name":"Curtin Medical School and Curtin Medical Research Institute, Curtin University, GPO Box U1987, Perth, WA 6845, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9191-5622","authenticated-orcid":false,"given":"Ricardo L.","family":"Mancera","sequence":"additional","affiliation":[{"name":"Curtin Medical School and Curtin Medical Research Institute, Curtin University, GPO Box U1987, Perth, WA 6845, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2025,2,6]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"391","DOI":"10.1002\/alz.12649","article-title":"The small HDL particle hypothesis of Alzheimer\u2019s disease","volume":"19","author":"Martinez","year":"2023","journal-title":"Alzheimer\u2019s Dement."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"555","DOI":"10.2217\/clp.10.37","article-title":"Apolipoproteins in the brain: Implications for neurological and psychiatric disorders","volume":"51","author":"Elliott","year":"2010","journal-title":"Clin. Lipidol."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"677","DOI":"10.3233\/JAD-150976","article-title":"Modulation of amyloid-\u03b21\u201340 transport by apoA1 and apoJ across an in vitro model of the blood-brain barrier","volume":"53","author":"Batlle","year":"2016","journal-title":"J. Alzheimer\u2019s Dis."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"1361","DOI":"10.1016\/j.biocel.2008.12.003","article-title":"Human apolipoprotein A\u2013I binds amyloid-\u03b2 and prevents A\u03b2-induced neurotoxicity","volume":"41","author":"Tricerri","year":"2009","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"36945","DOI":"10.1074\/jbc.M110.127738","article-title":"Apolipoprotein A-I deficiency increases cerebral amyloid angiopathy and cognitive deficits in APP\/PS1\u0394E9 mice","volume":"285","author":"Lefterov","year":"2010","journal-title":"J. Biol. Chem."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"32916","DOI":"10.1074\/jbc.271.51.32916","article-title":"Amyloid \u03b2-peptide is transported on lipoproteins and albumin in human plasma","volume":"271","author":"Biere","year":"1996","journal-title":"J. Biol. Chem."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"38570","DOI":"10.1074\/jbc.M111.260422","article-title":"Crystal structure of C-terminal truncated apolipoprotein A-I reveals the assembly of high density lipoprotein (HDL) by dimerization","volume":"286","author":"Mei","year":"2011","journal-title":"J. Biol. Chem."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"2966","DOI":"10.1074\/jbc.M110.163097","article-title":"Structure of apolipoprotein A-I N terminus on nascent high density lipoproteins","volume":"286","author":"Lagerstedt","year":"2011","journal-title":"J. Biol. Chem."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"1164","DOI":"10.1006\/bbrc.1994.2788","article-title":"The soluble form of Alzheimer\u2032s amyloid \u03b2 protein is complexed to high density lipoprotein 3 and very high density lipoprotein in normal human plasma","volume":"205","author":"Koudinov","year":"1994","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"5099","DOI":"10.1073\/pnas.0711731105","article-title":"Stabilization of a \u03b2-hairpin in monomeric Alzheimer\u2019s amyloid-\u03b2 peptide inhibits amyloid formation","volume":"105","author":"Hoyer","year":"2008","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"162","DOI":"10.1016\/j.jbiotec.2006.09.013","article-title":"Selection and characterization of affibody ligands binding to Alzheimer amyloid \u03b2 peptides","volume":"128","author":"Jonsson","year":"2007","journal-title":"J. Biotechnol."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"623","DOI":"10.1007\/s00775-014-1131-8","article-title":"The hairpin conformation of the amyloid \u03b2 peptide is an important structural motif along the aggregation pathway","volume":"19","author":"Abelein","year":"2014","journal-title":"J. Biol. Inorg. Chem."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"1581","DOI":"10.1110\/ps.041292205","article-title":"On the nucleation of amyloid \u03b2-protein monomer folding","volume":"14","author":"Lazo","year":"2005","journal-title":"Protein Sci."},{"key":"ref_14","doi-asserted-by":"crossref","unstructured":"Dubnovitsky, A., Sandberg, A., Rahman, M.M., Benilova, I., Lendel, C., and H\u00e4rd, T. (2013). Amyloid-\u03b2 protofibrils: Size, morphology and synaptotoxicity of an engineered mimic. PLoS ONE, 8.","DOI":"10.1371\/annotation\/44be8a39-d943-419b-a430-c2b30dafadec"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"15595","DOI":"10.1073\/pnas.1001740107","article-title":"Stabilization of neurotoxic Alzheimer amyloid-\u03b2 oligomers by protein engineering","volume":"107","author":"Sandberg","year":"2010","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"12756","DOI":"10.1002\/anie.201406357","article-title":"A hexameric peptide barrel as building block of amyloid-\u03b2 protofibrils","volume":"53","author":"Lendel","year":"2014","journal-title":"Angew. Chem. Int. Ed."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"766","DOI":"10.1021\/cb5008663","article-title":"Binding of human proteins to amyloid-\u03b2 protofibrils","volume":"10","author":"Rahman","year":"2014","journal-title":"ACS Chem. Biol."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"180","DOI":"10.1016\/j.drudis.2016.08.010","article-title":"Recombinant high-density lipoproteins and their use in cardiovascular diseases","volume":"22","author":"Cao","year":"2017","journal-title":"Drug Discov. Today"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"22123","DOI":"10.1016\/S0021-9258(18)45679-7","article-title":"Apolipoprotein A-I structure and lipid properties in homogeneous, reconstituted spherical and discoidal high density lipoproteins","volume":"265","author":"Jonas","year":"1990","journal-title":"J. Biol. Chem."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"2718","DOI":"10.1194\/jlr.M039206","article-title":"MD simulations suggest important surface differences between reconstituted and circulating spherical HDL","volume":"54","author":"Segrest","year":"2013","journal-title":"J. Lipid Res."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"2401","DOI":"10.1016\/j.bbamem.2016.03.010","article-title":"Computational studies of plasma lipoprotein lipids","volume":"1858","author":"Pan","year":"2016","journal-title":"BBA-Biomembranes"},{"key":"ref_22","doi-asserted-by":"crossref","unstructured":"Malajczuk, C.J., Gandhi, N.S., and Mancera, R.L. (2021). Structure and intermolecular interactions in spheroidal high-density lipoprotein subpopulations. J. Struct. Biol. X, 5.","DOI":"10.1016\/j.yjsbx.2020.100042"},{"key":"ref_23","doi-asserted-by":"crossref","unstructured":"Malajczuk, C.J., and Mancera, R.L. (2023). Unravelling the influence of surface lipids on the structure, dynamics and interactome of high-density lipoproteins. BBA-Biomembranes, 1865.","DOI":"10.1016\/j.bbamem.2023.184201"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"1116","DOI":"10.1016\/j.bpj.2024.03.039","article-title":"An atomistic characterization of high-density lipoproteins and the conserved \u201cLN\u201d region of apoA-I","volume":"123","author":"Malajczuk","year":"2024","journal-title":"Biophys. J."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"296","DOI":"10.1016\/0009-2614(95)00067-E","article-title":"Further evidence for a temperature-dependent hydrophobic interaction: The aggregation of ethane in aqueous solutions","volume":"234","author":"Mancera","year":"1995","journal-title":"Chem. Phys. Lett."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"2263","DOI":"10.1039\/a608381a","article-title":"The aggregation of methane in aqueous solution","volume":"93","author":"Mancera","year":"1997","journal-title":"J. Chem. Soc. Faraday Trans."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1039\/fd9960300141","article-title":"Computer simulation studies of the hydration and aggregation of simple hydrophobic molecules","volume":"103","author":"Skipper","year":"1996","journal-title":"Faraday Discuss."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"2960","DOI":"10.1016\/S0006-3495(97)78324-3","article-title":"Temperature, stability, and the hydrophobic interaction","volume":"73","author":"Schellman","year":"1997","journal-title":"Biophys. J."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"1555","DOI":"10.1002\/pro.435","article-title":"Temperature-dependent structural changes in intrinsically disordered proteins: Formation of alpha-helices or loss of polyproline II?","volume":"19","author":"Kjaergaard","year":"2010","journal-title":"Protein Sci."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"7916","DOI":"10.1021\/acs.jpcb.2c04743","article-title":"Characterization of the conformations of amyloid beta 42 in solution that may mediate its initial hydrophobic aggregation","volume":"126","author":"Sonar","year":"2022","journal-title":"J. Phys. Chem. B"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"1223","DOI":"10.2174\/13816128113199990068","article-title":"Inhibition of amyloid-\u03b2; aggregation in Alzheimer\u2019s disease","volume":"20","author":"Wang","year":"2014","journal-title":"Curr. Pharm. Des."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"19005","DOI":"10.1073\/pnas.0909708106","article-title":"Helical structure and stability in human apolipoprotein A-I by hydrogen exchange and mass spectrometry","volume":"106","author":"Chetty","year":"2009","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"1242","DOI":"10.1021\/bi051669r","article-title":"Structure and stability of apolipoprotein A-I in solution and in discoidal high density lipoprotein probed by double charge ablation and deletion mutation","volume":"45","author":"Gorshkova","year":"2006","journal-title":"Biochemistry"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"1221","DOI":"10.1016\/S0006-3495(92)81698-3","article-title":"Conformational analysis of apolipoprotein A-I and E-3 based on primary sequence and circular dichroism","volume":"63","author":"Nolte","year":"1992","journal-title":"Biophys. J."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1016\/S0014-5793(02)02600-5","article-title":"Heteronuclear NMR studies of human serum apolipoprotein A-I","volume":"517","author":"Okon","year":"2002","journal-title":"FEBS Lett."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"11687","DOI":"10.1073\/pnas.1209305109","article-title":"Apolipoprotein A-I helical structure and stability in discoidal high-density lipoprotein (HDL) particles by hydrogen exchange and mass spectrometry","volume":"109","author":"Chetty","year":"2012","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"2306","DOI":"10.1529\/biophysj.107.115857","article-title":"Structure of spheroidal HDL particles revealed by combined atomistic and coarse-grained simulations","volume":"94","author":"Catte","year":"2008","journal-title":"Biophys. J."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1194\/jlr.R012658","article-title":"Sequence conservation of apolipoprotein A-I affords novel insights into HDL structure-function","volume":"52","author":"Bashtovyy","year":"2011","journal-title":"J. Lipid Res."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"2249","DOI":"10.1021\/bi101301g","article-title":"\u201cSticky\u201d and \u201cpromiscuous\u201d\u2014The yin and yang of apolipoprotein A-I termini in discoidal high density lipoproteins: A combined computational-experimental approach","volume":"50","author":"Jones","year":"2011","journal-title":"Biochemistry"},{"key":"ref_40","doi-asserted-by":"crossref","unstructured":"Zannis, V.I., Fotakis, P., Koukos, G., Kardassis, D., Ehnholm, C., Jauhiainen, M., and Chroni, A. (2015). HDL biogenesis, remodeling, and catabolism. High Density Lipoproteins, Springer.","DOI":"10.1007\/978-3-319-09665-0_2"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1186\/1476-511X-8-46","article-title":"Amyloid-\u03b2 colocalizes with apolipoprotein B in absorptive cells of the small intestine","volume":"8","author":"Galloway","year":"2009","journal-title":"Lipids Health Dis."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"416","DOI":"10.1038\/nsmb.2028","article-title":"Apolipoprotein AI structural organization in high-density lipoproteins isolated from human plasma","volume":"18","author":"Huang","year":"2011","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"7882","DOI":"10.1021\/bi002734u","article-title":"Structure\u2212function relationships for inhibitors of \u03b2-amyloid toxicity containing the recognition sequence KLVFF","volume":"40","author":"Lowe","year":"2001","journal-title":"Biochemistry"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"17342","DOI":"10.1073\/pnas.0506723102","article-title":"3D structure of Alzheimer\u2019s amyloid-\u03b2(1\u201342) fibrils","volume":"102","author":"Ritter","year":"2005","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"16742","DOI":"10.1073\/pnas.262663499","article-title":"A structural model for Alzheimer\u2019s \u03b2-amyloid fibrils based on experimental constraints from solid state NMR","volume":"99","author":"Petkova","year":"2002","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"3234","DOI":"10.1039\/C9CP06188F","article-title":"Interaction of aliphatic amino acids with zwitterionic and charged lipid membranes: Hydration and dehydration phenomena","volume":"22","author":"Kanwa","year":"2020","journal-title":"Phys. Chem. Chem. Phys."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"2715","DOI":"10.1161\/ATVBAHA.113.301468","article-title":"Small, dense high-density lipoprotein-3 particles are enriched in negatively charged phospholipids: Relevance to cellular cholesterol efflux, antioxidative, antithrombotic, anti-inflammatory, and antiapoptotic functionalities","volume":"33","author":"Camont","year":"2013","journal-title":"Arterioscler. Thromb. Vasc. Biol."},{"key":"ref_48","doi-asserted-by":"crossref","unstructured":"Anantharamaiah, G.M., and Goldberg, D. (2015). HDL and the Amphipathic Helix. Apolipoprotein Mimetics in the Management of Human Disease, Springer International Publishing.","DOI":"10.1007\/978-3-319-17350-4"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1021\/ct700301q","article-title":"GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation","volume":"4","author":"Hess","year":"2008","journal-title":"J. Chem. Theory Comput."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"11405","DOI":"10.1021\/acs.jpcb.6b08685","article-title":"Tautomeric effect of histidine on the monomeric structure of amyloid \u03b2-peptide (1\u201340)","volume":"120","author":"Shi","year":"2016","journal-title":"J. Phys. Chem. B"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"843","DOI":"10.1007\/s00249-011-0700-9","article-title":"Definition and testing of the GROMOS force-field versions 54A7 and 54B7","volume":"40","author":"Schmid","year":"2011","journal-title":"Eur. Biophys. J."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"1656","DOI":"10.1002\/jcc.20090","article-title":"A biomolecular force field based on the free enthalpy of hydration and solvation: The GROMOS force-field parameter sets 53A5 and 53A6","volume":"25","author":"Oostenbrink","year":"2004","journal-title":"J. Comput. Chem."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"4026","DOI":"10.1021\/ct200196m","article-title":"An Automated Force Field Topology Builder (ATB) and repository: Version 1.0","volume":"7","author":"Malde","year":"2011","journal-title":"J. Chem. Theory Comput."},{"key":"ref_54","doi-asserted-by":"crossref","unstructured":"Berendsen, H.J., Postma, J.P., van Gunsteren, W.F., and Hermans, J. (1981). Interaction models for water in relation to protein hydration. Intermolecular Forces, Springer.","DOI":"10.1007\/978-94-015-7658-1_21"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"2587","DOI":"10.1021\/acs.jcim.5b00308","article-title":"Force-field induced bias in the structure of A\u03b221\u201330: A comparison of OPLS, AMBER, CHARMM, and GROMOS force fields","volume":"55","author":"Smith","year":"2015","journal-title":"J. Chem. Inf. Model."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"2796","DOI":"10.1002\/jcc.23459","article-title":"Refinement of the application of the GROMOS 54A7 force field to \u03b2-peptides","volume":"34","author":"Lin","year":"2013","journal-title":"J. Comput. Chem."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"1237","DOI":"10.1021\/ct100747y","article-title":"Validation of the GROMOS 54A7 force field with respect to \u03b2-peptide folding","volume":"7","author":"Huang","year":"2011","journal-title":"J. Chem. Theory Comput."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"2562","DOI":"10.1002\/hlca.201200534","article-title":"Validation of the GROMOS 54A7 force field regarding mixed \u03b1\/\u03b2-peptide molecules","volume":"95","author":"Wang","year":"2012","journal-title":"Helv. Chim. Acta"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"15943","DOI":"10.1021\/jp407536p","article-title":"Conformational Biases of Linear Motifs","volume":"117","author":"Cino","year":"2013","journal-title":"J. Phys. Chem. B"},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"2073","DOI":"10.1039\/b716554d","article-title":"A temperature predictor for parallel tempering simulations","volume":"10","author":"Patriksson","year":"2008","journal-title":"Phys. Chem. Chem. Phys."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"17765","DOI":"10.1073\/pnas.0602632103","article-title":"Secondary structure provides a template for the folding of nearby polypeptides","volume":"103","author":"Kameda","year":"2006","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"511","DOI":"10.1063\/1.447334","article-title":"A unified formulation of the constant temperature molecular dynamics methods","volume":"81","year":"1984","journal-title":"J. Chem. Phys."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"1695","DOI":"10.1103\/PhysRevA.31.1695","article-title":"Canonical dynamics: Equilibrium phase-space distributions","volume":"31","author":"Hoover","year":"1985","journal-title":"Phys. Rev. A"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"7182","DOI":"10.1063\/1.328693","article-title":"Polymorphic transitions in single crystals: A new molecular dynamics method","volume":"52","author":"Parrinello","year":"1981","journal-title":"J. Appl. Phys."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"10089","DOI":"10.1063\/1.464397","article-title":"Particle mesh Ewald: An N log (N) method for Ewald sums in large systems","volume":"98","author":"Darden","year":"1993","journal-title":"J. Chem. Phys."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"1463","DOI":"10.1002\/(SICI)1096-987X(199709)18:12<1463::AID-JCC4>3.0.CO;2-H","article-title":"LINCS: A linear constraint solver for molecular simulations","volume":"18","author":"Hess","year":"1997","journal-title":"J. Comput. Chem."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1021\/la00037a043","article-title":"A molecular dynamics study of the structure and dynamics of water between dilauroylphosphatidylethanolamine bilayers","volume":"8","author":"Raghavan","year":"1992","journal-title":"Langmuir"},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"236","DOI":"10.1002\/(SICI)1521-3773(19990115)38:1\/2<236::AID-ANIE236>3.0.CO;2-M","article-title":"Peptide folding: When simulation meets experiment","volume":"38","author":"Daura","year":"1999","journal-title":"Angew. Chem. Int. Ed."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"1951","DOI":"10.1021\/ci500020m","article-title":"g_mmpbsa\u2014A GROMACS Tool for High-Throughput MM-PBSA Calculations","volume":"54","author":"Kumari","year":"2014","journal-title":"J. Chem. Inf. Model."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"460","DOI":"10.1016\/0022-2836(92)90835-8","article-title":"Substitutions of hydrophobic amino acids reduce the amyloidogenicity of Alzheimer\u2019s disease \u03b2A4 peptides","volume":"228","author":"Hilbich","year":"1992","journal-title":"J. Mol. Biol."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"12601","DOI":"10.1074\/jbc.272.19.12601","article-title":"Controlling amyloid \u03b2-peptide fibril formation with protease-stable ligands","volume":"272","author":"Tjernberg","year":"1997","journal-title":"J. Biol. Chem."},{"key":"ref_72","doi-asserted-by":"crossref","unstructured":"Castelletto, V., Ryumin, P., Cramer, R., Hamley, I., Taylor, M., Allsop, D., Reza, M., Ruokolainen, J., Arnold, T., and Hermida-Merino, D. (2017). Self-assembly and anti-amyloid cytotoxicity activity of amyloid beta peptide derivatives. Sci. Rep., 7.","DOI":"10.1038\/srep43637"},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"814","DOI":"10.1016\/j.jcis.2022.01.051","article-title":"KLVFF oligopeptide-decorated amphiphilic cyclodextrin nanomagnets for selective amyloid beta recognition and fishing","volume":"613","author":"Mazzaglia","year":"2022","journal-title":"J. Colloid Interface Sci."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"1972","DOI":"10.1016\/j.drudis.2021.04.011","article-title":"Nanotechnological approaches for targeting amyloid-\u03b2 aggregation with potential for neurodegenerative disease therapy and diagnosis","volume":"26","author":"Shukla","year":"2021","journal-title":"Drug Discov. Today"},{"key":"ref_75","doi-asserted-by":"crossref","unstructured":"Ciccone, L., Shi, C., di Lorenzo, D., Van Baelen, A.-C., and Tonali, N. (2020). The positive side of the Alzheimer\u2019s disease amyloid cross-interactions: The case of the A\u03b2 1-42 peptide with tau, TTR, CysC, and ApoA1. Molecules, 25.","DOI":"10.3390\/molecules25102439"}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/26\/3\/1380\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,9]],"date-time":"2025-10-09T16:28:08Z","timestamp":1760027288000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/26\/3\/1380"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,2,6]]},"references-count":75,"journal-issue":{"issue":"3","published-online":{"date-parts":[[2025,2]]}},"alternative-id":["ijms26031380"],"URL":"https:\/\/doi.org\/10.3390\/ijms26031380","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,2,6]]}}}