{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,5]],"date-time":"2026-08-05T00:55:50Z","timestamp":1785891350962,"version":"3.56.0"},"reference-count":66,"publisher":"MDPI AG","issue":"5","license":[{"start":{"date-parts":[[2016,5,2]],"date-time":"2016-05-02T00:00:00Z","timestamp":1462147200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["SFB TRR 102, projects A3 and A6"],"award-info":[{"award-number":["SFB TRR 102, projects A3 and A6"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Polymers"],"abstract":"<jats:p>The formation of amyloid fibrils is considered to be one of the main causes for many neurodegenerative diseases, such as Alzheimer\u2019s, Parkinson\u2019s or Huntington\u2019s disease. Current knowledge suggests that amyloid-aggregation represents a nucleation-dependent aggregation process in vitro, where a sigmoidal growth phase follows an induction period. Here, we studied the fibrillation of amyloid \u03b2 1-40 (A\u03b240) in the presence of thermoresponsive polymers, expected to alter the A\u03b240 fibrillation kinetics due to their lower critical solution behavior. To probe the influence of molecular weight and the end groups of the polymer on its lower critical solution temperature (LCST), also considering its concentration dependence in the presence of buffer-salts needed for the aggregation studies of the amyloids, poly(oxazolines) (POx) with LCSTs ranging from 14.2\u201349.8 \u00b0C and poly(methoxy di(ethylene glycol)acrylates) with LCSTs ranging from 34.4\u201352.7 \u00b0C were synthesized. The two different polymers allowed the comparison of the influence of different molecular structures onto the fibrillation process. Mixtures of A\u03b240 with these polymers in varying concentrations were studied via time-dependent measurements of the thioflavin T (ThT) fluorescence. The studies revealed that amyloid fibrillation was accelerated in, accompanied by an extension of the lag phase of A\u03b240 fibrillation from 18.3 h in the absence to 19.3 h in the presence of the poly(methoxy di(ethylene glycol)acrylate) (3600 g\/mol).<\/jats:p>","DOI":"10.3390\/polym8050178","type":"journal-article","created":{"date-parts":[[2016,5,2]],"date-time":"2016-05-02T10:17:11Z","timestamp":1462184231000},"page":"178","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":19,"title":["Amyloid Beta Aggregation in the Presence of Temperature-Sensitive Polymers"],"prefix":"10.3390","volume":"8","author":[{"given":"Sebastian","family":"Funtan","sequence":"first","affiliation":[{"name":"Faculty of Natural Science II, Martin-Luther University Halle-Wittenberg, Von-Danckelmann-Platz 4, D-06120 Halle (Saale), Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zhanna","family":"Evgrafova","sequence":"additional","affiliation":[{"name":"Faculty of Natural Science II, Martin-Luther University Halle-Wittenberg, Von-Danckelmann-Platz 4, D-06120 Halle (Saale), Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Juliane","family":"Adler","sequence":"additional","affiliation":[{"name":"Institute for Medical Physics and Biophysics, Leipzig University, H\u00e4rtelstra\u00dfe 16-18, D-04107 Leipzig, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daniel","family":"Huster","sequence":"additional","affiliation":[{"name":"Institute for Medical Physics and Biophysics, Leipzig University, H\u00e4rtelstra\u00dfe 16-18, D-04107 Leipzig, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3834-5445","authenticated-orcid":false,"given":"Wolfgang","family":"Binder","sequence":"additional","affiliation":[{"name":"Faculty of Natural Science II, Martin-Luther University Halle-Wittenberg, Von-Danckelmann-Platz 4, D-06120 Halle (Saale), Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2016,5,2]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1146\/annurev.biochem.75.101304.123901","article-title":"Protein misfolding, functional amyloid, and human disease","volume":"75","author":"Chiti","year":"2006","journal-title":"Annu. Rev. Biochem."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"8128","DOI":"10.1002\/anie.200700861","article-title":"Peptide fibrillization","volume":"46","author":"Hamley","year":"2007","journal-title":"Angew. Chem. Int. Ed."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"5147","DOI":"10.1021\/cr3000994","article-title":"The amyloid beta peptide: A chemist\u2019s perspective. Role in alzheimer\u2019s and fibrillization","volume":"112","author":"Hamley","year":"2012","journal-title":"Chem. Rev."},{"key":"ref_4","doi-asserted-by":"crossref","unstructured":"Sgarbossa, A. (2012). Natural biomolecules and protein aggregation: Emerging strategies against amyloidogenesis. Int. J. Mol. Sci.","DOI":"10.3390\/ijms131217121"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1021\/ja408765u","article-title":"Quantification of the concentration of a\u03b242 propagons during the lag phase by an amyloid chain reaction assay","volume":"136","author":"Arosio","year":"2014","journal-title":"J. Am. Chem. Soc."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"9384","DOI":"10.1073\/pnas.1401564111","article-title":"Differences in nucleation behavior underlie the contrasting aggregation kinetics of the A\u03b240 and A\u03b242 peptides","volume":"111","author":"Meisl","year":"2014","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_7","unstructured":"Sackler, A.M. (2002). Self-Perpetuating Structural States in Biology, Disease, and Genetics, National Academy of Sciences."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"1137","DOI":"10.1021\/ma202157h","article-title":"Proteins fibrils from a polymer physics perspective","volume":"45","author":"Adamcik","year":"2012","journal-title":"Macromolecules"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"2837","DOI":"10.1002\/anie.201007265","article-title":"Solid-state NMR spectroscopic investigation of A\u03b2 protofibrils: Implication of a \u03b2-sheet remodeling upon maturation into terminal amyloid fibrils","volume":"50","author":"Scheidt","year":"2011","journal-title":"Angew. Chem. Int. Ed."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"1157","DOI":"10.1038\/nsmb1345","article-title":"Evidence of fibril-like \u03b2-sheet structures in a neurotoxic amyloid intermediate of Alzheimer\u2019s \u03b2-amyloid","volume":"14","author":"Chimon","year":"2007","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1016\/j.bbrc.2006.04.041","article-title":"Influence of dendrimer\u2019s structure on its activity against amyloid fibril formation","volume":"345","author":"Klajnert","year":"2006","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"591","DOI":"10.1016\/0022-2836(85)90174-3","article-title":"Kinetics of sickle hemoglobin polymerization: I. Studies using temperature-jump and laser photolysis techniques","volume":"183","author":"Ferrone","year":"1985","journal-title":"J. Mol. Biol."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"611","DOI":"10.1016\/0022-2836(85)90175-5","article-title":"Kinetics of sickle hemoglobin polymerization: II. A double nucleation mechanism","volume":"183","author":"Ferrone","year":"1985","journal-title":"J. Mol. Biol."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"160","DOI":"10.1016\/j.jmb.2012.02.031","article-title":"From macroscopic measurements to microscopic mechanisms of protein aggregation","volume":"421","author":"Cohen","year":"2012","journal-title":"J. Mol. Biol."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1038\/nsmb.2971","article-title":"A molecular chaperone breaks the catalytic cycle that generates toxic A\u03b2 oligomers","volume":"22","author":"Cohen","year":"2015","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"10311","DOI":"10.1074\/jbc.M608207200","article-title":"Small molecule inhibitors of aggregation indicate that amyloid \u03b2 oligomerization and fibrillization pathways are independent and distinct","volume":"282","author":"Necula","year":"2007","journal-title":"J. Biol. Chem."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1016\/j.jmb.2011.12.062","article-title":"Inhibition of amyloid formation","volume":"421","author":"Lendel","year":"2012","journal-title":"J. Mol. Biol."},{"key":"ref_18","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_19","doi-asserted-by":"crossref","first-page":"7873","DOI":"10.1021\/ja075356q","article-title":"Design of an n-methylated peptide inhibitor of \u03b1-synuclein aggregation guided by solid-state NMR","volume":"130","author":"Madine","year":"2008","journal-title":"J. Am. Chem. Soc."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"28163","DOI":"10.1074\/jbc.C112.360800","article-title":"Human serum albumin can regulate amyloid-\u03b2 peptide fiber growth in the brain interstitium: Implications for Alzheimer disease","volume":"287","author":"Stanyon","year":"2012","journal-title":"J. Biol. Chem."},{"key":"ref_21","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_22","doi-asserted-by":"crossref","first-page":"764","DOI":"10.1006\/bbrc.2002.6514","article-title":"Poly-l-lysine dissolves fibrillar aggregation of the alzheimer \u03b2-amyloid peptide in vitro","volume":"291","author":"Nguyen","year":"2002","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"2186","DOI":"10.1021\/bm060229s","article-title":"Molecular interactions of dendrimers with amyloid peptides: pH dependence","volume":"7","author":"Klajnert","year":"2006","journal-title":"Biomacromolecules"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"1047","DOI":"10.1002\/mabi.200700051","article-title":"Dendrimer effects on peptide and protein fibrillation","volume":"7","author":"Heegaard","year":"2007","journal-title":"Macromol. Biosci."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"15437","DOI":"10.1021\/ja8041806","article-title":"Inhibition of amyloid \u03b2 protein fibrillation by polymeric nanoparticles","volume":"130","author":"Lynch","year":"2008","journal-title":"J. Am. Chem. Soc."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"279","DOI":"10.1021\/cn900027u","article-title":"Dual effect of amino modified polystyrene nanoparticles on amyloid \u03b2 protein fibrillation","volume":"1","author":"Lynch","year":"2010","journal-title":"ACS Chem. Neurosci."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"2662","DOI":"10.1021\/bm3011177","article-title":"Engineered polymer nanoparticles containing hydrophobic dipeptide for inhibition of amyloid-\u03b2 fibrillation","volume":"13","author":"Skaat","year":"2012","journal-title":"Biomacromolecules"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"2206","DOI":"10.1016\/j.bpj.2010.01.063","article-title":"Retardation of A\u03b2 fibril formation by phospholipid vesicles depends on membrane phase behavior","volume":"98","author":"Hellstrand","year":"2010","journal-title":"Biophys. J."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"755","DOI":"10.1006\/jmbi.1998.2348","article-title":"Solution structures of micelle-bound amyloid \u03b2-(1-40) and \u03b2-(1-42) peptides of Alzheimer\u2019s disease","volume":"285","author":"Shao","year":"1999","journal-title":"J. Mol. Biol."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"12451","DOI":"10.1021\/bi701213s","article-title":"Amyloid-\u03b2(1-42) rapidly forms protofibrils and oligomers by distinct pathways in low concentrations of sodium dodecylsulfate","volume":"46","author":"Rangachari","year":"2007","journal-title":"Biochemistry"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"3913","DOI":"10.1039\/b908203d","article-title":"Aggregation structure of alzheimer amyloid-\u03b2(1\u201340) peptide with sodium dodecyl sulfate as revealed by small-angle X-ray and neutron scattering","volume":"5","author":"Lin","year":"2009","journal-title":"Soft Matter"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"23518","DOI":"10.1074\/jbc.M113.470450","article-title":"Formation of dynamic soluble surfactant-induced amyloid \u03b2 peptide aggregation intermediates","volume":"288","author":"Abelein","year":"2013","journal-title":"J. Biol. Chem."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"1852","DOI":"10.1021\/la203078w","article-title":"The effect of nanoparticles on amyloid aggregation depends on the protein stability and intrinsic aggregation rate","volume":"28","author":"Szczepankiewicz","year":"2012","journal-title":"Langmuir"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"21630","DOI":"10.1021\/jp505613g","article-title":"Inhibition of amyloid fibril growth by nanoparticle coated with histidine-based polymer","volume":"118","author":"Palmal","year":"2014","journal-title":"J. Phys. Chem. C"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"8812","DOI":"10.1021\/la501414j","article-title":"Effects of polyamino acids and polyelectrolytes on amyloid \u03b2 fibril formation","volume":"30","author":"Assarsson","year":"2014","journal-title":"Langmuir"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"5839","DOI":"10.1039\/c3sm50428j","article-title":"Thermoresponsive self-assembled polymer colloids in water","volume":"9","author":"Hocine","year":"2013","journal-title":"Soft Matter"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"1441","DOI":"10.1080\/10601326808051910","article-title":"Solution properties of poly(N-isopropylacrylamide)","volume":"2","author":"Heskins","year":"1968","journal-title":"J. Macromol. Sci. A"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"3311","DOI":"10.1021\/j100345a085","article-title":"Phase transition of aqueous solutions of poly(N-isopropylacrylamide) and poly(N-isopropylmethacrylamide)","volume":"93","author":"Fujishige","year":"1989","journal-title":"J. Phys. Chem."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1016\/S0141-8130(99)00122-1","article-title":"On the temperature-induced coil to globule transition of poly-N-isopropylacrylamide in dilute aqueous solutions","volume":"27","author":"Graziano","year":"2000","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"603","DOI":"10.1002\/polb.1988.090260312","article-title":"Solubility and miscibility of poly(ethyl oxazoline)","volume":"26","author":"Lin","year":"1988","journal-title":"J. Polym. Sci. B Polym. Phys."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"1643","DOI":"10.1246\/cl.1992.1643","article-title":"A novel thermo-sensitive polymer. Poly(2-iso-propyl-2-oxazoline)","volume":"21","author":"Uyama","year":"1992","journal-title":"Chem. Lett."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"3599","DOI":"10.1021\/ma0701181","article-title":"Comprehensive and accurate control of thermosensitivity of poly(2-alkyl-2-oxazoline)s via well-defined gradient or random copolymerization","volume":"40","author":"Park","year":"2007","journal-title":"Macromolecules"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"7978","DOI":"10.1002\/anie.200901607","article-title":"Poly(2-oxazoline)s: A polymer class with numerous potential applications","volume":"48","author":"Hoogenboom","year":"2009","journal-title":"Angew. Chem. Int. Ed."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"1173","DOI":"10.1016\/j.progpolymsci.2004.08.003","article-title":"Stimuli-reponsive polymers and their bioconjugates","volume":"29","author":"Gil","year":"2004","journal-title":"Prog. Polym. Sci."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1007\/12_2010_57","article-title":"Non-ionic thermoresponsive polymers in water","volume":"242","author":"Aseyev","year":"2011","journal-title":"Adv. Polym. Sci."},{"key":"ref_46","doi-asserted-by":"crossref","unstructured":"Hoogenboom, R., Thijs, H.M.L., Jochems, M.J.H.C., van Lankvelt, B.M., Fijten, M.W.M., and Schubert, U.S. (2008). Tuning the lcst of poly(2-oxazoline)s by varying composition and molecular weight: Alternatives to poly(N-isopropylacrylamide)?. Chem. Commun., 5758\u20135760.","DOI":"10.1039\/b813140f"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"395","DOI":"10.1007\/s00396-007-1781-y","article-title":"Modulation of the lower critical solution temperature of 2-alkyl-2-oxazoline copolymers","volume":"286","author":"Huber","year":"2008","journal-title":"Colloid Polym. Sci."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"3118","DOI":"10.1002\/pola.27364","article-title":"Tuning the lcst of poly(2-cyclopropyl-2-oxazoline) via gradient copolymerization with 2-ethyl-2-oxazoline","volume":"52","author":"Glassner","year":"2014","journal-title":"J. Polym. Sci. A Polym. Chem."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"2275","DOI":"10.1021\/ma0519617","article-title":"End group effect on the thermal response of narrow-disperse poly(N-isopropylacrylamide) prepared by atom transfer radical polymerization","volume":"39","author":"Xia","year":"2006","journal-title":"Macromolecules"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"1653","DOI":"10.1007\/s00396-008-1942-7","article-title":"Effect of end group polarity upon the lower critical solution temperature of poly(2-isopropyl-2-oxazoline)","volume":"286","author":"Huber","year":"2008","journal-title":"Colloid Polym. Sci."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"42","DOI":"10.1021\/ma021257f","article-title":"Synthesis of water-soluble polymethacrylates by living anionic polymerization of trialkylsilyl-protected oligo(ethylene glycol) methacrylates","volume":"36","author":"Ishizone","year":"2003","journal-title":"Macromolecules"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"7461","DOI":"10.1039\/C3CP54501F","article-title":"Local interactions influence the fibrillation kinetics, structure and dynamics of A\u03b2(1\u201340) but leave the general fibril structure unchanged","volume":"16","author":"Adler","year":"2014","journal-title":"Phys. Chem. Chem. Phys."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"6036","DOI":"10.1021\/bi002555c","article-title":"Effect of environmental factors on the kinetics of insulin fibril formation: Elucidation of the molecular mechanism\u2020","volume":"40","author":"Nielsen","year":"2001","journal-title":"Biochemistry"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"4144","DOI":"10.1021\/la063048k","article-title":"Thioflavin t and birefringence assays to determine the conversion of proteins into fibrils","volume":"23","author":"Bolder","year":"2007","journal-title":"Langmuir"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"6786","DOI":"10.1021\/ma049677n","article-title":"Versatile synthesis of end-functionalized thermosensitive poly(2-isopropyl-2-oxazolines)","volume":"37","author":"Park","year":"2004","journal-title":"Macromolecules"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"996","DOI":"10.1002\/jlac.197419740615","article-title":"Cyclische imids\u00e4ureester aus nitrilen und aminoalkoholen","volume":"1974","author":"Witte","year":"1974","journal-title":"Justus Liebigs Ann. Chem."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"569","DOI":"10.1007\/s00396-011-2384-1","article-title":"Collapse transition in thin films of poly(methoxydiethylenglycol acrylate)","volume":"289","author":"Zhong","year":"2011","journal-title":"Colloid Polym. Sci."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"5602","DOI":"10.1039\/C4PY01224K","article-title":"Polymer-protein conjugation via a \u2018grafting to\u2019 approach\u2014A comparative study of the performance of protein-reactive raft chain transfer agents","volume":"6","author":"Vanparijs","year":"2015","journal-title":"Polym. Chem."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"2454","DOI":"10.1002\/pola.21357","article-title":"Well-defined thermosensitive, water-soluble polyacrylates and polystyrenics with short pendant oligo(ethylene glycol) groups synthesized by nitroxide-mediated radical polymerization","volume":"44","author":"Hua","year":"2006","journal-title":"J. Polym. Sci. A Polym. Chem."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"2191","DOI":"10.1021\/ma048787r","article-title":"Ab initio emulsion polymerization by raft-controlled self-assembly","volume":"38","author":"Ferguson","year":"2005","journal-title":"Macromolecules"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1021\/acs.macromol.5b02279","article-title":"Influence of hydrophobic polystyrene blocks on the rehydration of polystyrene-block-poly(methoxy diethylene glycol acrylate)-block-polystyrene films investigated by in situ neutron reflectivity","volume":"49","author":"Zhong","year":"2016","journal-title":"Macromolecules"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"3313","DOI":"10.1002\/pola.26116","article-title":"Influencing the phase transition temperature of poly(methoxy diethylene glycol acrylate) by molar mass, end groups, and polymer architecture","volume":"50","author":"Miasnikova","year":"2012","journal-title":"J. Polym. Sci. Part A"},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"2255","DOI":"10.1016\/S0032-3861(03)00139-3","article-title":"New thermo-responsive polymer materials based on poly(2-ethyl-2-oxazoline) segments","volume":"44","author":"Christova","year":"2003","journal-title":"Polymer"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"12806","DOI":"10.1021\/bi0610653","article-title":"Nature and significance of the interactions between amyloid fibrils and biological polyelectrolytes","volume":"45","author":"Calamai","year":"2006","journal-title":"Biochemistry"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1021\/cn900015v","article-title":"Amyloid \u03b2-protein aggregation produces highly reproducible kinetic data and occurs by a two-phase process","volume":"1","author":"Hellstrand","year":"2010","journal-title":"ACS Chem. Neurosci."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"3775","DOI":"10.1021\/la404739f","article-title":"Complexation of amyloid fibrils with charged conjugated polymers","volume":"30","author":"Ghosh","year":"2014","journal-title":"Langmuir"}],"container-title":["Polymers"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2073-4360\/8\/5\/178\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T19:23:11Z","timestamp":1760210591000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2073-4360\/8\/5\/178"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2016,5,2]]},"references-count":66,"journal-issue":{"issue":"5","published-online":{"date-parts":[[2016,5]]}},"alternative-id":["polym8050178"],"URL":"https:\/\/doi.org\/10.3390\/polym8050178","relation":{},"ISSN":["2073-4360"],"issn-type":[{"value":"2073-4360","type":"electronic"}],"subject":[],"published":{"date-parts":[[2016,5,2]]}}}