{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,17]],"date-time":"2026-06-17T08:58:31Z","timestamp":1781686711840,"version":"3.54.5"},"reference-count":114,"publisher":"MDPI AG","issue":"12","license":[{"start":{"date-parts":[[2026,6,17]],"date-time":"2026-06-17T00:00:00Z","timestamp":1781654400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Physiologically produced circulating \u03b2-amyloid (A\u03b2) exerts critical physiological functions. Although A\u03b2 is a key player in Alzheimer\u2019s disease (AD), it may initially be beneficial at the onset of infection. As an evolutionary conserved antimicrobial peptide (AMP), A\u03b2 contributes to innate immune defense against pathogens. Host defense peptides such as A\u03b2 and human cathelicidin (LL-37) not only kill pathogens through their antimicrobial activity but also exhibit high affinity for bacterial lipopolysaccharides (LPSs) and membrane receptors. LL-37, which is upregulated in the brain, binds to A\u03b2, modulating its aggregation; A\u03b2 and LL-37 are protective under physiological conditions, but during chronic infection or dysregulation, their interaction becomes toxic and contributes to AD pathology. Similarly to A\u03b2, LL-37 can induce neuroinflammation by stimulating human microglia to release inflammatory cytokines, such as TNF-\u03b1 and IL-6. Neuroinflammation is essential for protecting the brain from pathogens\u2014when prolonged, it drives pathological processes underlying AD, Parkinson\u2019s disease (PD), and other neurodegenerative disorders.<\/jats:p>","DOI":"10.3390\/ijms27125460","type":"journal-article","created":{"date-parts":[[2026,6,17]],"date-time":"2026-06-17T08:22:56Z","timestamp":1781684576000},"page":"5460","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["\u03b2-Amyloid (A\u03b2) and Human Cathelicidin LL-37: Two Sides of the Same Coin?"],"prefix":"10.3390","volume":"27","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-3605-1283","authenticated-orcid":false,"given":"Anna Lia","family":"Asti","sequence":"first","affiliation":[{"name":"Department of Medical and Surgical Sciences, Alma Mater Studiorum, Universit\u00e0 di Bologna, 40126 Bologna, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2026,6,17]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"28551","DOI":"10.1016\/S0021-9258(19)61939-3","article-title":"Surfactant properties of Alzheimer\u2019s A beta peptides and the mechanism of amyloid aggregation","volume":"269","author":"Soreghan","year":"1994","journal-title":"J. Biol. Chem."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"921","DOI":"10.1016\/S0896-6273(00)80115-4","article-title":"Mechanisms of neuronal degeneration in Alzheimer\u2019s disease","volume":"16","author":"Yankner","year":"1996","journal-title":"Neuron"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1056\/NEJMra023144","article-title":"Molecular Mechanisms of Amyloidosis","volume":"349","author":"Merlini","year":"2003","journal-title":"N. Engl. J. Med."},{"key":"ref_4","doi-asserted-by":"crossref","unstructured":"Sun, X., Chen, W.D., and Wang, Y.D. (2015). \u03b2-Amyloid: The key peptide in the pathogenesis of Alzheimer\u2019s disease. Front. Pharmacol., 6.","DOI":"10.3389\/fphar.2015.00221"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"5481","DOI":"10.1038\/s41380-021-01249-0","article-title":"The Amyloid-\u03b2 Pathway in Alzheimer\u2019s Disease","volume":"26","author":"Hampel","year":"2021","journal-title":"Mol. Psychiatry"},{"key":"ref_6","doi-asserted-by":"crossref","unstructured":"Soscia, S.J., Kirby, J.E., Washicosky, K.J., Tucker, S.M., Ingelsson, M., Hyman, B., Burton, M.A., Goldstein, L.E., Duong, S., and Tanzi, R.E. (2010). The Alzheimer\u2019s disease-associated amyloid beta-protein is an antimicrobial peptide. PLoS ONE, 5.","DOI":"10.1371\/journal.pone.0009505"},{"key":"ref_7","doi-asserted-by":"crossref","unstructured":"Mahlapuu, M., H\u00e5kansson, J., Ringstad, L., and Bj\u00f6rn, C. (2016). Antimicrobial Peptides: An Emerging Category of Therapeutic Agents. Front. Cell. Infect. Microbiol., 6.","DOI":"10.3389\/fcimb.2016.00194"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1016\/j.bcp.2015.02.003","article-title":"Human antimicrobial peptide LL-37 induces glial-mediated neuroinflammation","volume":"94","author":"Lee","year":"2015","journal-title":"Biochem. Pharmacol."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"32637","DOI":"10.1074\/jbc.M805533200","article-title":"Structures of human host defense cathelicidin LL-37 and its smallest antimicrobial peptide KR-12 in lipid micelles","volume":"283","author":"Wang","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"1033","DOI":"10.1006\/jmbi.2000.3908","article-title":"The protofilament substructure of amyloid Brils","volume":"300","author":"Serpell","year":"2000","journal-title":"J. Mol. Biol."},{"key":"ref_11","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_12","doi-asserted-by":"crossref","first-page":"2102978","DOI":"10.1002\/adfm.202102978","article-title":"Design and Engineering of Amyloid Aggregation-Prone Fragments and Their Antimicrobial Conjugates with Multi-Target Functionality","volume":"31","author":"Zhang","year":"2021","journal-title":"Adv. Funct. Mater."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1016\/S0140-6736(06)69113-7","article-title":"Alzheimer\u2019s disease","volume":"368","author":"Blennow","year":"2006","journal-title":"Lancet"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"4749","DOI":"10.1074\/jbc.R800036200","article-title":"Amyloid \u03b2-Protein Assembly and Alzheimer Disease","volume":"284","author":"Roychaudhuri","year":"2009","journal-title":"J. Biol. Chem."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"340ra72","DOI":"10.1126\/scitranslmed.aaf1059","article-title":"Amyloid-\u03b2 peptide protects against microbial infection in mouse and worm models of Alzheimer\u2019s disease","volume":"8","author":"Kumar","year":"2016","journal-title":"Sci. Transl. Med."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"1125","DOI":"10.1073\/pnas.93.3.1125","article-title":"On the nucleation and growth of amyloid beta-protein fibrils: Detection of nuclei and quantitation of rate constants","volume":"93","author":"Lomakin","year":"1996","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_17","doi-asserted-by":"crossref","unstructured":"Brown, M.R., Radford, S.E., and Hewitt, E.W. (2020). Modulation of \u03b2-Amyloid Fibril Formation in Alzheimer\u2019s Disease by Microglia and Infection. Front. Mol. Neurosci., 13.","DOI":"10.3389\/fnmol.2020.609073"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"6323","DOI":"10.1021\/bi5008172","article-title":"The binding of apolipoprotein E to oligomers and fibrils of amyloid-\u03b2 alters the kinetics of amyloid aggregation","volume":"53","author":"Garai","year":"2014","journal-title":"Biochemistry"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"106429","DOI":"10.1016\/j.bpc.2020.106429","article-title":"Self-assembly of surfactants: An overview on general aspects of amphiphiles","volume":"265","author":"Ghosh","year":"2020","journal-title":"Biophys. Chem."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"5401","DOI":"10.1021\/ja00408a021","article-title":"Formation of stable bilayer assemblies in water from single-chain amphiphiles. Relationship between the amphiphile structure and the aggregate morphology","volume":"103","author":"Kunitake","year":"1981","journal-title":"J. Am. Chem. Soc."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"169","DOI":"10.3233\/JAD-131394","article-title":"Can a bacterial endotoxin be a key factor in the kinetic of amyloid fibril formation?","volume":"39","author":"Asti","year":"2014","journal-title":"J. Alzheimer\u2019s Dis."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"614","DOI":"10.1007\/s12035-012-8320-7","article-title":"Infectious agents and neurodegeneration","volume":"46","author":"Marcocci","year":"2012","journal-title":"Mol. Neurobiol."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"1602","DOI":"10.1016\/j.jalz.2018.06.3040","article-title":"The antimicrobial protection hypothesis of Alzheimer\u2019s disease","volume":"14","author":"Moir","year":"2018","journal-title":"Alzheimer\u2019s Dement."},{"key":"ref_24","doi-asserted-by":"crossref","unstructured":"Stroffolini, G., Guastamacchia, G., Audagnotto, S., Atzori, C., Trunfio, M., Nigra, M., Di Stefano, A., Di Perri, G., and Calcagno, A. (2021). Low cerebrospinal fluid Amyloid-\u03b2eta 1-42 in patients with tuberculous meningitis. BMC Neurol., 21.","DOI":"10.1186\/s12883-021-02468-2"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1556\/1886.2024.00035","article-title":"Methods for screening and evaluation of antimicrobial activity: A review of protocols, advantages, and limitations","volume":"14","author":"Hossain","year":"2024","journal-title":"Eur. J. Microbiol. Immunol."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"1989","DOI":"10.1097\/00001756-200210280-00032","article-title":"Amyloid beta peptide induces cytochrome C release from isolated mitochondria","volume":"13","author":"Kim","year":"2002","journal-title":"Neuroreport"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"e30","DOI":"10.1017\/S1462399411002006","article-title":"Emerging roles of pathogens in Alzheimer disease","volume":"13","author":"Miklossy","year":"2011","journal-title":"Expert Rev. Mol. Med."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"553","DOI":"10.1016\/S0014-4886(03)00365-0","article-title":"The emerging role of infectious pathogens in neurodegenerative diseases","volume":"184","author":"Langford","year":"2003","journal-title":"Exp. Neurol."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1007\/s10571-014-0101-6","article-title":"Microglial A\u03b2 receptors in Alzheimer\u2019s disease","volume":"35","author":"Yu","year":"2015","journal-title":"Cell. Mol. Neurobiol."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"54","DOI":"10.1038\/s41380-023-02053-8","article-title":"Human antimicrobial peptide LL-37 contributes to Alzheimer\u2019s disease progression","volume":"29","author":"Chen","year":"2024","journal-title":"Mol. Psychiatry"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"2236","DOI":"10.1016\/j.immuni.2022.10.016","article-title":"Emerging roles of innate and adaptive immunity in Alzheimer\u2019s disease","volume":"55","author":"Chen","year":"2022","journal-title":"Immunity"},{"key":"ref_32","unstructured":"Janeway, C.A., Travers, P., Walport, M., and Shlomchik, M.J. (2001). Principles of innate and adaptive immunity. Immunobiology: The Immune System in Health and Disease, Garland Science. [5th ed.]."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1111\/j.1365-2990.1996.tb00839.x","article-title":"David Oppenheimer Memorial Lecture 1995: Some neuropathological aspects of Alzheimer\u2019s disease and its relevance to other disciplines","volume":"22","author":"Wisniewski","year":"1996","journal-title":"Neuropathol. Appl. Neurobiol."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"707","DOI":"10.1016\/j.neurobiolaging.2006.12.001","article-title":"Degradation of fibrillar forms of Alzheimer\u2019s amyloid beta-peptide by macrophages","volume":"29","author":"Majumdar","year":"2008","journal-title":"Neurobiol. Aging"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"48","DOI":"10.5056\/jnm18087","article-title":"Brain-Gut-Microbiota Axis in Alzheimer\u2019s Disease","volume":"25","author":"Kowalski","year":"2019","journal-title":"J. Neurogastroenterol. Motil."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"939","DOI":"10.3233\/JAD-210268","article-title":"NLRP3 Inflammasome: A Starring Role in Amyloid-\u03b2- and Tau-Driven Pathological Events in Alzheimer\u2019s Disease","volume":"83","author":"Dias","year":"2021","journal-title":"J. Alzheimer\u2019s Dis."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1038\/ni.3102","article-title":"Innate immunity in Alzheimer\u2019s disease","volume":"16","author":"Heneka","year":"2015","journal-title":"Nat. Immunol."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"2470","DOI":"10.2174\/1568026611212220003","article-title":"Aggregation prone regions and gatekeeping residues in protein sequences","volume":"12","author":"Beerten","year":"2012","journal-title":"Curr. Top. Med. Chem."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1042\/bse0560041","article-title":"Predicting aggregation-prone sequences in proteins","volume":"56","author":"Perrett","year":"2014","journal-title":"Essays Biochem."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"1302","DOI":"10.1038\/nbt1012","article-title":"Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins","volume":"22","author":"Rousseau","year":"2004","journal-title":"Nat. Biotechnol."},{"key":"ref_41","doi-asserted-by":"crossref","unstructured":"Buck, P.M., Kumar, S., and Singh, S.K. (2013). On the role of aggregation prone regions in protein evolution, stability, and enzymatic catalysis: Insights from diverse analyses. PLoS Comput. Biol., 9.","DOI":"10.1371\/journal.pcbi.1003291"},{"key":"ref_42","doi-asserted-by":"crossref","unstructured":"Castillo, V., and Ventura, S. (2009). Amyloidogenic regions and interaction surfaces overlap in globular proteins related to conformational diseases. PLoS Comput. Biol., 5.","DOI":"10.1371\/journal.pcbi.1000476"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"1512","DOI":"10.1007\/s11095-010-0143-5","article-title":"Potential aggregation-prone regions in complementarity-determining regions of antibodies and their contribution towards antigen recognition: A computational analysis","volume":"27","author":"Wang","year":"2010","journal-title":"Pharm. Res."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"866","DOI":"10.1038\/s41467-018-03131-0","article-title":"Aggregating sequences that occur in many proteins constitute weak spots of bacterial proteostasis","volume":"9","author":"Khodaparast","year":"2018","journal-title":"Nat. Commun."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"1408","DOI":"10.1016\/j.bbamem.2006.03.030","article-title":"LL-37, the only human member of the cathelicidin family of antimicrobial peptides","volume":"1758","author":"Sudheendra","year":"2006","journal-title":"Biochim. Biophys. Acta."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"17356","DOI":"10.1038\/s41598-020-74401-5","article-title":"The structure of the antimicrobial human cathelicidin LL-37 shows oligomerization and channel formation in the presence of membrane mimics","volume":"10","author":"Bonetti","year":"2020","journal-title":"Sci. Rep."},{"key":"ref_47","first-page":"1187","article-title":"Bacterial lipopolysaccharide and antimicrobial LL-37 enhance ICAM-1 expression and NF-\u03baB p65 phosphorylation in senescent endothelial cells","volume":"44","author":"Suzuki","year":"2019","journal-title":"Int. J. Mol. Med."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"3894","DOI":"10.1038\/s41467-020-17736-x","article-title":"The Human LL-37(17-29) antimicrobial peptide reveals a functional supramolecular structure","volume":"11","author":"Engelberg","year":"2020","journal-title":"Nat. Commun."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"1213","DOI":"10.3233\/JAD-170223","article-title":"Evidence that the Human Innate Immune Peptide LL-37 may be a Binding Partner of Amyloid-\u03b2 and Inhibitor of Fibril Assembly","volume":"59","author":"Chiari","year":"2017","journal-title":"J. Alzheimer\u2019s Dis."},{"key":"ref_50","doi-asserted-by":"crossref","unstructured":"Bhattacharjya, S., Zhang, Z., and Ramamoorthy, A. (2024). LL-37: Structures, Antimicrobial Activity, and Influence on Amyloid-Related Diseases. Biomolecules, 14.","DOI":"10.3390\/biom14030320"},{"key":"ref_51","doi-asserted-by":"crossref","unstructured":"Pahar, B., Madonna, S., Das, A., Albanesi, C., and Girolomoni, G. (2020). Immunomodulatory Role of the Antimicrobial LL-37 Peptide in Autoimmune Diseases and Viral Infections. Vaccines, 8.","DOI":"10.3390\/vaccines8030517"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"e172578","DOI":"10.1172\/JCI172578","article-title":"Increased LL37 in psoriasis and other inflammatory disorders promote LDL uptake and atherosclerosis","volume":"134","author":"Nakamura","year":"2024","journal-title":"J. Clin. Investig."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"5565","DOI":"10.1021\/bi702036s","article-title":"NMR structure of the cathelicidin-derived human antimicrobial peptide LL-37 in dodecylphosphocholine micelles","volume":"47","author":"Porcelli","year":"2008","journal-title":"Biochemistry"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"670","DOI":"10.1089\/aid.2013.0279","article-title":"LL-37 concentrations and the relationship to vitamin D, immune status, and inflammation in HIV-infected children and young adults","volume":"30","author":"Tangpricha","year":"2014","journal-title":"AIDS Res. Hum. Retroviruses"},{"key":"ref_55","doi-asserted-by":"crossref","unstructured":"Aloul, K.M., Nielsen, J.E., Defensor, E.B., Lin, J.S., Fortkort, J.A., Shamloo, M., Cirillo, J.D., Gombart, A.F., and Barron, A.E. (2022). Upregulating Human Cathelicidin Antimicrobial Peptide LL-37 Expression May Prevent Severe COVID-19 Inflammatory Responses and Reduce Microthrombosis. Front. Immunol., 13.","DOI":"10.3389\/fimmu.2022.880961"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"304","DOI":"10.1016\/j.immuni.2015.07.013","article-title":"Pancreatic \u03b2-Cells Limit Autoimmune Diabetes via an Immunoregulatory Antimicrobial Peptide Expressed under the Influence of the Gut Microbiota","volume":"43","author":"Sun","year":"2015","journal-title":"Immunity"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"327","DOI":"10.1111\/j.1600-0625.2012.01459.x","article-title":"Cathelicidin LL-37: A defense molecule with a potential role in psoriasis pathogenesis","volume":"21","author":"Dombrowski","year":"2012","journal-title":"Exp. Dermatol."},{"key":"ref_58","doi-asserted-by":"crossref","unstructured":"Fan, H., Sun, R., Ma, Q., Li, X., Liu, J., Zhang, M., Xu, C., Zhang, D., and Ma, W. (2025). LL37-driven mast cell degranulation and inflammation in rosacea via TLR2\/JAK2\/STAT3 axis. Front. Immunol., 16.","DOI":"10.3389\/fimmu.2025.1672021"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"118568","DOI":"10.1016\/j.biopha.2025.118568","article-title":"Neutrophils and NETosis in Alzheimer\u2019s disease: Unraveling pathogenic mechanisms and novel therapeutic targets","volume":"192","author":"Chavoshinezhad","year":"2025","journal-title":"Biomed. Pharmacother."},{"key":"ref_60","doi-asserted-by":"crossref","unstructured":"Radic, M., and Muller, S. (2022). LL-37, a Multi-Faceted Amphipathic Peptide Involved in NETosis. Cells, 11.","DOI":"10.3390\/cells11152463"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"336","DOI":"10.1007\/s12035-025-05435-x","article-title":"NETosis in Alzheimer\u2019s Disease: Understanding the Role of Neutrophil Extracellular Traps (NETs) in Neuroinflammation and Disease Pathogenesis","volume":"63","author":"Rao","year":"2026","journal-title":"Mol. Neurobiol."},{"key":"ref_62","doi-asserted-by":"crossref","unstructured":"Gryka-Marton, M., Grabowska, A.D., and Szukiewicz, D. (2025). Breaking the Barrier: The Role of Proinflammatory Cytokines in BBB Dysfunction. Int. J. Mol. Sci., 26.","DOI":"10.3390\/ijms26083532"},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"151865","DOI":"10.1016\/j.imbio.2019.10.014","article-title":"The emerging role of neutrophils in neurodegeneration","volume":"225","author":"Rossi","year":"2020","journal-title":"Immunobiology"},{"key":"ref_64","doi-asserted-by":"crossref","unstructured":"Chakraborty, S., Tabrizi, Z., Bhatt, N.N., Franciosa, S.A., and Bracko, O. (2023). A Brief Overview of Neutrophils in Neurological Diseases. Biomolecules, 13.","DOI":"10.3390\/biom13050743"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1358\/dof.2017.042.01.2564104","article-title":"Targeting neuroinflammation in the treatment and prevention of Alzheimer\u2019s disease","volume":"42","author":"Zenaro","year":"2017","journal-title":"Drugs Future"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"12575","DOI":"10.1074\/jbc.272.19.12575","article-title":"Molecular cloning and expression of a chloride ion channel of cell nuclei","volume":"272","author":"Valenzuela","year":"1997","journal-title":"J. Biol. Chem."},{"key":"ref_67","doi-asserted-by":"crossref","unstructured":"Carlini, V., Verduci, I., Cianci, F., Cannavale, G., Fenoglio, C., Galimberti, D., and Mazzanti, M. (2020). CLIC1 Protein Accumulates in Circulating Monocyte Membrane during Neurodegeneration. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21041484"},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"C1103","DOI":"10.1152\/ajpcell.00402.2001","article-title":"CLIC1 inserts from the aqueous phase into phospholipid membranes, where it functions as an anion channel","volume":"282","author":"Tulk","year":"2002","journal-title":"Am. J. Physiol. Cell Physiol."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"15493","DOI":"10.1074\/jbc.274.22.15493","article-title":"beta-amyloid activates the O-2 forming NADPH oxidase in microglia, monocytes, and neutrophils. A possible inflammatory mechanism of neuronal damage in Alzheimer\u2019s disease","volume":"274","author":"Bianca","year":"1999","journal-title":"J. Biol. Chem."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"30","DOI":"10.1186\/1742-2094-3-30","article-title":"The microglial NADPH oxidase complex as a source of oxidative stress in Alzheimer\u2019s disease","volume":"3","author":"Wilkinson","year":"2006","journal-title":"J. Neuroinflamm."},{"key":"ref_71","doi-asserted-by":"crossref","unstructured":"F\u00fcl\u00f6p, T., Itzhaki, R.F., Balin, B.J., Miklossy, J., and Barron, A.E. (2018). Role of Microbes in the Development of Alzheimer\u2019s Disease: State of the Art\u2014An International Symposium Presented at the 2017 IAGG Congress in San Francisco. Front. Genet., 9.","DOI":"10.3389\/fgene.2018.00362"},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"2284","DOI":"10.1523\/JNEUROSCI.17-07-02284.1997","article-title":"Amyloid fibrils activate tyrosine kinase-dependent signaling and superoxide production in microglia","volume":"17","author":"McDonald","year":"1997","journal-title":"J. Neurosci."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"4064","DOI":"10.1529\/biophysj.106.097766","article-title":"Role of electrostatic interactions in amyloid beta-protein (A beta) oligomer formation: A discrete molecular dynamics study","volume":"92","author":"Yun","year":"2007","journal-title":"Biophys. J."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"e75889","DOI":"10.7554\/eLife.75889","article-title":"LL-37 expression reduces acute and chronic neuroinflammation and rescues cognitive impairment in an Alzheimer\u2019s disease mouse model","volume":"11","author":"Lonnemann","year":"2022","journal-title":"eLife"},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1007\/s00109-006-0143-4","article-title":"Multifunctional antimicrobial peptides: Therapeutics targets in several human diseases","volume":"85","author":"Zaiou","year":"2007","journal-title":"J. Mol. Med."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1038\/nrm2101","article-title":"Soluble protein oligomers in neurodegeneration: Lessons from Alzheimer\u2019s amyloid beta-peptide","volume":"8","author":"Haass","year":"2007","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"421","DOI":"10.3233\/JAD-2008-13407","article-title":"Infection and Alzheimer\u2019s disease: The APOE epsilon4 connection and lipid metabolism","volume":"13","author":"Urosevic","year":"2008","journal-title":"J. Alzheimer\u2019s Dis."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"1637","DOI":"10.1016\/j.neurobiolaging.2006.07.007","article-title":"Genetic risk profiles for Alzheimer\u2019s disease: Integration of APOE genotype and variants that up-regulate inflammation","volume":"28","author":"Licastro","year":"2007","journal-title":"Neurobiol. Aging"},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"2586","DOI":"10.1021\/acschemneuro.4c00084","article-title":"Preparation and Characterization of Zn(II)-Stabilized A\u03b242 Oligomers","volume":"15","author":"Mannini","year":"2024","journal-title":"ACS Chem. Neurosci."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"975","DOI":"10.3233\/JAD-160612","article-title":"Amyloid-Beta and Phosphorylated Tau Accumulations Cause Abnormalities at Synapses of Alzheimer\u2019s disease Neurons","volume":"57","author":"Rajmohan","year":"2017","journal-title":"J. Alzheimer\u2019s Dis."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"9477","DOI":"10.1038\/s41598-020-66373-3","article-title":"A Novel A\u03b240 Assembly at Physiological Concentration","volume":"10","author":"Tahirbegi","year":"2020","journal-title":"Sci. Rep."},{"key":"ref_82","doi-asserted-by":"crossref","unstructured":"Gursky, O. (2015). Lipids in Protein Misfolding. Advances in Experimental Medicine and Biology 855, Springer International Publishing.","DOI":"10.1007\/978-3-319-17344-3"},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"609","DOI":"10.1016\/S0968-4328(02)00029-X","article-title":"In vitro fibrillogenesis of the amyloid beta 1-42 peptide: Cholesterol potentiation and aspirin inhibition","volume":"33","author":"Harris","year":"2002","journal-title":"Micron"},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"1013","DOI":"10.1016\/j.bbamem.2011.09.008","article-title":"Folding and misfolding of alpha-synuclein on membranes","volume":"1818","author":"Dikiy","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1007\/s00249-007-0237-0","article-title":"How is protein aggregation in amyloidogenic diseases modulated by biological membranes?","volume":"37","author":"Aisenbrey","year":"2008","journal-title":"Eur. Biophys. J."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"9595","DOI":"10.1074\/jbc.M411805200","article-title":"Structure and dynamics of micelle-bound human alpha-synuclein","volume":"280","author":"Ulmer","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1016\/j.bbagen.2017.06.004","article-title":"Dynamic membrane interactions of antibacterial and antifungal biomolecules, and amyloid peptides, revealed by solid-state NMR spectroscopy","volume":"1862","author":"Naito","year":"2018","journal-title":"Biochim. Biophys. Acta Gen. Subj."},{"key":"ref_88","doi-asserted-by":"crossref","unstructured":"Skrzypczak-Wiercioch, A., and Sa\u0142at, K. (2022). Lipopolysaccharide-Induced Model of Neuroinflammation: Mechanisms of Action, Research Application and Future Directions for Its Use. Molecules, 27.","DOI":"10.3390\/molecules27175481"},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"5376","DOI":"10.1038\/s41598-024-55423-9","article-title":"Mechanistic insights into the role of amyloid-\u03b2 in innate immunity","volume":"14","author":"Prosswimmer","year":"2024","journal-title":"Sci. Rep."},{"key":"ref_90","doi-asserted-by":"crossref","unstructured":"Zhan, X., Stamova, B., and Sharp, F.R. (2018). Lipopolysaccharide Associates with Amyloid Plaques, Neurons and Oligodendrocytes in Alzheimer\u2019s Disease Brain: A Review. Front. Aging Neurosci., 10.","DOI":"10.3389\/fnagi.2018.00042"},{"key":"ref_91","unstructured":"Calne, D. (1994). Bacteria and neurodegeneration. Neurodegenerative Diseases, W.B. Saunders Company."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"180","DOI":"10.1186\/s12974-019-1564-7","article-title":"The endotoxin hypothesis of neurodegeneration","volume":"16","author":"Brown","year":"2019","journal-title":"J. Neuroinflamm."},{"key":"ref_93","doi-asserted-by":"crossref","unstructured":"Rodr\u00edguez-G\u00f3mez, J.A., Kavanagh, E., Engskog-Vlachos, P., Engskog, M.K., Herrera, A.J., Espinosa-Oliva, A.M., Joseph, B., Hajji, N., Venero, J.L., and Burguillos, M.A. (2020). Microglia: Agents of the CNS Pro-Inflammatory Response. Cells, 9.","DOI":"10.3390\/cells9071717"},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1007\/s004300050071","article-title":"Identification and localization of Chlamydia pneumoniae in the Alzheimer\u2019s brain","volume":"187","author":"Balin","year":"1998","journal-title":"Med. Microbiol. Immunol."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"2324","DOI":"10.1212\/WNL.0000000000003391","article-title":"Gram-negative bacterial molecules associate with Alzheimer disease pathology","volume":"87","author":"Zhan","year":"2016","journal-title":"Neurology"},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1002\/(SICI)1098-1136(20000101)29:1<1::AID-GLIA1>3.0.CO;2-N","article-title":"Production of nitric oxide by glial cells: Regulation and potential roles in the CNS","volume":"29","author":"Murphy","year":"2000","journal-title":"Glia"},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"1017","DOI":"10.1073\/pnas.1814924116","article-title":"Rigidification of the Escherichia coli cytoplasm by the human antimicrobial peptide LL-37 revealed by superresolution fluorescence microscopy","volume":"116","author":"Zhu","year":"2019","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"412","DOI":"10.1111\/j.1600-051X.2011.01710.x","article-title":"Edotoxemia and the host systemic response during experimental gingivitis","volume":"38","author":"Wahaidi","year":"2011","journal-title":"J. Clin. Periodontol."},{"key":"ref_99","doi-asserted-by":"crossref","unstructured":"Noble, J.M., Scarmeas, N., Celenti, R.S., Elkind, M.S.V., Wright, C.B., Schupf, N., and Papapanou, P.N. (2014). Serum IgG antibody levels to periodontal microbiota are associated with incident Alzheimer disease. PLoS ONE, 9.","DOI":"10.1371\/journal.pone.0114959"},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"627","DOI":"10.1016\/j.neurobiolaging.2014.10.038","article-title":"Periodontal disease associates with higher brain amyloid load in normal elderly","volume":"36","author":"Kamer","year":"2015","journal-title":"Neurobiol. Aging"},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"29143","DOI":"10.3402\/jom.v7.29143","article-title":"Can oral infection be a risk factor for Alzheimer\u2019s disease?","volume":"7","author":"Olsen","year":"2015","journal-title":"J. Oral Microbiol."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"178","DOI":"10.1038\/nature11319","article-title":"Gut microbiota composition correlates with diet and health in the elderly","volume":"488","author":"Claesson","year":"2012","journal-title":"Nature"},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"734","DOI":"10.3892\/mmr.2021.12374","article-title":"Roles of \u03b1-synuclein in gastrointestinal microbiome dysbiosis-related Parkinson\u2019s disease progression (Review)","volume":"24","author":"Lei","year":"2021","journal-title":"Mol. Med. Rep."},{"key":"ref_104","doi-asserted-by":"crossref","unstructured":"Adamu, A., Li, S., Gao, F., and Xue, G. (2024). The role of neuroinflammation in neurodegenerative diseases: Current understanding and future therapeutic targets. Front. Aging Neurosci., 16.","DOI":"10.3389\/fnagi.2024.1347987"},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"299","DOI":"10.1016\/bs.pmbts.2019.06.002","article-title":"Can infections trigger alpha-synucleinopathies?","volume":"168","author":"Tulisiak","year":"2019","journal-title":"Prog. Mol. Biol. Transl. Sci."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"e1392","DOI":"10.20883\/medical.e1392","article-title":"Extracellular matrix, amyloid fibrils and infections. Is there a new approach to combat amyloidosis?","volume":"95","author":"Asti","year":"2026","journal-title":"J. Med. Sci."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"1143","DOI":"10.1002\/mds.29432","article-title":"The Endotoxin Hypothesis of Parkinson\u2019s Disease","volume":"38","author":"Brown","year":"2023","journal-title":"Mov. Disord."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"1469","DOI":"10.1016\/j.cell.2016.11.018","article-title":"Gut Microbiota Regulate Motor Deficits and Neuroinflammation in a Model of Parkinson\u2019s Disease","volume":"167","author":"Sampson","year":"2016","journal-title":"Cell"},{"key":"ref_109","doi-asserted-by":"crossref","unstructured":"Liu, B., Zhang, H., and Qin, X. (2025). Amyloid Fibrils and Their Applications: Current Status and Latest Developments. Nanomaterials, 15.","DOI":"10.3390\/nano15040255"},{"key":"ref_110","doi-asserted-by":"crossref","unstructured":"Bruno, F., Malvaso, A., Canterini, S., and Bruni, A.C. (2022). Antimicrobial Peptides (AMPs) in the Pathogenesis of Alzheimer\u2019s Disease: Implications for Diagnosis and Treatment. Antibiotics, 11.","DOI":"10.20944\/preprints202205.0166.v1"},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"33457","DOI":"10.1021\/acsami.3c06599","article-title":"Amyloid-Inspired Engineered Multidomain Amphiphilic Injectable Peptide Hydrogel\u2500An Excellent Antibacterial, Angiogenic, and Biocompatible Wound Healing Material","volume":"15","author":"Mukherjee","year":"2023","journal-title":"ACS Appl. Mater. Interfaces"},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"7711","DOI":"10.1007\/s00253-022-12246-w","article-title":"Amyloid peptides with antimicrobial and\/or microbial agglutination activity","volume":"106","author":"Chen","year":"2022","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"184439","DOI":"10.1016\/j.bbamem.2025.184439","article-title":"Development of amyloid-cationic peptides with antimicrobial activities: Relation to their membranotropic activities","volume":"1867","author":"Balestra","year":"2025","journal-title":"Biochim. Biophys. Acta (BBA)\u2014Biomembr."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"e70490","DOI":"10.1002\/alz.70490","article-title":"Human amylin is a potent antimicrobial peptide that exhibits antimicrobial synergism with the amyloid beta protein","volume":"21","author":"Mitchell","year":"2025","journal-title":"Alzheimer\u2019s Dement."}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/27\/12\/5460\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,6,17]],"date-time":"2026-06-17T08:27:46Z","timestamp":1781684866000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/27\/12\/5460"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,6,17]]},"references-count":114,"journal-issue":{"issue":"12","published-online":{"date-parts":[[2026,6]]}},"alternative-id":["ijms27125460"],"URL":"https:\/\/doi.org\/10.3390\/ijms27125460","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,6,17]]}}}