{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,20]],"date-time":"2026-10-20T12:42:38Z","timestamp":1792500158963,"version":"4.5.0"},"reference-count":80,"publisher":"American Chemical Society (ACS)","issue":"20","license":[{"start":{"date-parts":[[2026,9,8]],"date-time":"2026-09-08T00:00:00Z","timestamp":1788825600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2026,9,8]],"date-time":"2026-09-08T00:00:00Z","timestamp":1788825600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2026,9,8]],"date-time":"2026-09-08T00:00:00Z","timestamp":1788825600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-045"}],"funder":[{"DOI":"10.13039\/501100001843","name":"Science and Engineering Research Board","doi-asserted-by":"publisher","award":["SRG\/2023\/001243"],"award-info":[{"award-number":["SRG\/2023\/001243"]}],"id":[{"id":"10.13039\/501100001843","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100012025","name":"New York University Abu Dhabi","doi-asserted-by":"publisher","award":["AD389"],"award-info":[{"award-number":["AD389"]}],"id":[{"id":"10.13039\/100012025","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,10,20]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Misfolding and aggregation of islet amyloid polypeptide (IAPP) are associated with the decline of \u03b2-cells in type 2 diabetes (T2D). Design of short peptide-based inhibitors of \u03b2-sheet-rich amyloid plaque formation is challenging due to the dynamic nature of the amyloid species. The key sequences involved in cross-amyloid interactions shed light on the design of peptide-based inhibitors. Amyloid-\u03b2 peptide (A\u03b2) has nearly 50% similarity and 25% identity with IAPP sequences, and their cross-interactions have been suggested to link T2D pathogenesis with Alzheimer\u2019s disease (AD). Here, we show that a short anionic amphiphilic hexapeptide (DM-P02) containing the A\u03b2 domain (Leu17\u2013Glu22) effectively suppresses aggregation and oligomerization of IAPP by predominantly interacting with its cationic N-terminus. DM-P02 also binds strongly to IAPP in pancreatic \u03b2-cell lines, as confirmed by confocal imaging, and protects them from IAPP aggregation-associated cytotoxicity. Our study underlines the therapeutic potential of short peptides for developing anti-amyloid agents.<\/jats:p>","DOI":"10.1021\/acs.biochem.6c00469","type":"journal-article","created":{"date-parts":[[2026,9,8]],"date-time":"2026-09-08T13:01:48Z","timestamp":1788872508000},"page":"3226-3235","source":"Crossref","is-referenced-by-count":0,"title":["A\u03b217\u201322 Derived Hexapeptide\nSegment Inhibits Islet Amyloid Polypeptide (IAPP) Aggregation and\nAttenuates Cytotoxicity"],"prefix":"10.1021","volume":"65","author":[{"given":"Subhadip","family":"Jana","sequence":"first","affiliation":[{"name":"CSIR-Indian Institute of Chemical Technology (CSIR-IICT) , , ,","place":["Hyderabad, India, 500007"]},{"name":"Academy of Scientific and Innovative Research (AcSIR) , ,","place":["Ghaziabad, India, 201002"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sk Rajibul","family":"Haque","sequence":"additional","affiliation":[{"name":"CSIR-Indian Institute of Chemical Technology (CSIR-IICT) , , ,","place":["Hyderabad, India, 500007"]},{"name":"Academy of Scientific and Innovative Research (AcSIR) , ,","place":["Ghaziabad, India, 201002"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2639-0436","authenticated-orcid":true,"given":"Loganathan","family":"Palanikumar","sequence":"additional","affiliation":[{"name":"New York University Abu Dhabi , , P.O. Box 129188, Saadiyat Island Campus , ,","place":["Abu Dhabi, United Arab Emirates, 00000"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gabriel D.","family":"Verley","sequence":"additional","affiliation":[{"name":"New York University Abu Dhabi , , P.O. Box 129188, Saadiyat Island Campus , ,","place":["Abu Dhabi, United Arab Emirates, 00000"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rudra Shankar","family":"Das","sequence":"additional","affiliation":[{"name":"CSIR-Indian Institute of Chemical Technology (CSIR-IICT) , , ,","place":["Hyderabad, India, 500007"]},{"name":"Academy of Scientific and Innovative Research (AcSIR) , ,","place":["Ghaziabad, India, 201002"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sagarika","family":"Patra","sequence":"additional","affiliation":[{"name":"CSIR-Indian Institute of Chemical Technology (CSIR-IICT) , , ,","place":["Hyderabad, India, 500007"]},{"name":"Academy of Scientific and Innovative Research (AcSIR) , ,","place":["Ghaziabad, India, 201002"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3414-6617","authenticated-orcid":true,"given":"Mazin","family":"Magzoub","sequence":"additional","affiliation":[{"name":"New York University Abu Dhabi , , P.O. Box 129188, Saadiyat Island Campus , ,","place":["Abu Dhabi, United Arab Emirates, 00000"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4301-3106","authenticated-orcid":true,"given":"Debabrata","family":"Maity","sequence":"additional","affiliation":[{"name":"CSIR-Indian Institute of Chemical Technology (CSIR-IICT) , , ,","place":["Hyderabad, India, 500007"]},{"name":"Academy of Scientific and Innovative Research (AcSIR) , ,","place":["Ghaziabad, India, 201002"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2026,9,8]]},"reference":[{"key":"2026102007161022500_cit1","doi-asserted-by":"publisher","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."},{"issue":"7","key":"2026102007161022500_cit2","doi-asserted-by":"publisher","first-page":"439","DOI":"10.1016\/j.molmed.2015.04.005","article-title":"Type 2 diabetes as\na protein misfolding disease","volume":"21","author":"Mukherjee","year":"2015","journal-title":"Trends Mol. Med."},{"issue":"12","key":"2026102007161022500_cit3","doi-asserted-by":"publisher","first-page":"755","DOI":"10.1038\/s41580-018-0060-8","article-title":"A new era\nfor understanding amyloid structures and disease","volume":"19","author":"Iadanza","year":"2018","journal-title":"Nat. Rev. Mol. Cell Biol."},{"issue":"13","key":"2026102007161022500_cit4","doi-asserted-by":"publisher","first-page":"8285","DOI":"10.1021\/acs.chemrev.1c00196","article-title":"Amyloid-type\nProtein Aggregation and Prion-like Properties of Amyloids","volume":"121","author":"Willbold","year":"2021","journal-title":"Chem. Rev."},{"issue":"6","key":"2026102007161022500_cit5","doi-asserted-by":"publisher","first-page":"438","DOI":"10.1002\/1097-0282(2001)60:6","article-title":"Amyloidogenicity\nand cytotoxicity of islet amyloid polypeptide","volume":"60","author":"Kapurniotu","year":"2001","journal-title":"Pept. Sci."},{"issue":"1","key":"2026102007161022500_cit6","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-021-23985-1","article-title":"Protein mimetic amyloid inhibitor potently\nabrogates cancer-associated mutant p53 aggregation and restores tumor\nsuppressor function","volume":"12","author":"Palanikumar","year":"2021","journal-title":"Nat. Commun."},{"issue":"2","key":"2026102007161022500_cit7","doi-asserted-by":"publisher","DOI":"10.1016\/j.xcrp.2020.100014","article-title":"Designed Cell-Penetrating\nPeptide Inhibitors of Amyloid-beta Aggregation and Cytotoxicity","volume":"1","author":"Henning-Knechtel","year":"2020","journal-title":"Cell Rep. Phys. Sci."},{"issue":"3","key":"2026102007161022500_cit8","doi-asserted-by":"publisher","first-page":"795","DOI":"10.1152\/physrev.00042.2009","article-title":"Islet Amyloid Polypeptide, Islet\nAmyloid, and Diabetes Mellitus","volume":"91","author":"Westermark","year":"2011","journal-title":"Physiol. Rev."},{"issue":"13","key":"2026102007161022500_cit9","doi-asserted-by":"publisher","first-page":"5036","DOI":"10.1073\/pnas.87.13.5036","article-title":"Islet amyloid polypeptide: pinpointing amino acid residues\nlinked to amyloid fibril formation","volume":"87","author":"Westermark","year":"1990","journal-title":"Proc. Natl.\nAcad. Sci. U.S.A."},{"issue":"3","key":"2026102007161022500_cit10","doi-asserted-by":"publisher","first-page":"1845","DOI":"10.1021\/acs.chemrev.0c00981","article-title":"Proteostasis\nof Islet Amyloid Polypeptide:\nA Molecular Perspective of Risk Factors and Protective Strategies\nfor Type II Diabetes","volume":"121","author":"Milardi","year":"2021","journal-title":"Chem. Rev."},{"key":"2026102007161022500_cit11","doi-asserted-by":"publisher","DOI":"10.7554\/eLife.31226","article-title":"Stabilization and structural\nanalysis of a membrane-associated hIAPP aggregation intermediate","volume":"6","author":"Rodriguez Camargo","year":"2017","journal-title":"eLife"},{"issue":"25","key":"2026102007161022500_cit12","doi-asserted-by":"publisher","first-page":"4679","DOI":"10.1002\/anie.200705372","article-title":"Small-Molecule Inhibitors of Islet Amyloid Polypeptide\nFibril Formation","volume":"47","author":"Mishra","year":"2008","journal-title":"Angew. Chem., Int. Ed."},{"issue":"7","key":"2026102007161022500_cit13","doi-asserted-by":"publisher","first-page":"1632","DOI":"10.1021\/cb500162w","article-title":"Aspirin, Diabetes,\nand Amyloid: Re-examination of the Inhibition of Amyloid Formation\nby Aspirin and Ketoprofen","volume":"9","author":"Tu","year":"2014","journal-title":"ACS Chem. Biol."},{"issue":"1","key":"2026102007161022500_cit14","doi-asserted-by":"publisher","first-page":"73","DOI":"10.1038\/nchem.2129","article-title":"Screening\nand classifying small-molecule inhibitors of amyloid formation using\nion mobility spectrometry\u2013mass spectrometry","volume":"7","author":"Young","year":"2015","journal-title":"Nat. Chem."},{"issue":"5","key":"2026102007161022500_cit15","doi-asserted-by":"publisher","first-page":"942","DOI":"10.1039\/C5CC07792C","article-title":"Influence of a curcumin derivative on hIAPP aggregation\nin the absence and presence of lipid membranes","volume":"52","author":"Pithadia","year":"2016","journal-title":"Chem. Commun."},{"issue":"14","key":"2026102007161022500_cit16","doi-asserted-by":"publisher","first-page":"11859","DOI":"10.1021\/jacs.4c16743","article-title":"Kinetic Steering\nof Amyloid Formation and Polymorphism by Canagliflozin, a Type-2 Diabetes\nDrug","volume":"147","author":"Taylor","year":"2025","journal-title":"J. Am. Chem. 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Diabetes Res."},{"issue":"42","key":"2026102007161022500_cit19","doi-asserted-by":"publisher","first-page":"16958","DOI":"10.1021\/ja206279b","article-title":"Lysine-Specific Molecular\nTweezers Are Broad-Spectrum Inhibitors of Assembly and Toxicity of\nAmyloid Proteins","volume":"133","author":"Sinha","year":"2011","journal-title":"J. Am. Chem. Soc."},{"issue":"38","key":"2026102007161022500_cit20","doi-asserted-by":"publisher","DOI":"10.1002\/chem.202200456","article-title":"Cucurbit[7]uril\nInhibits Islet Amyloid Polypeptide Aggregation by Targeting N Terminus\nHot Segments and Attenuates Cytotoxicity","volume":"28","author":"Maity","year":"2022","journal-title":"Chem.\n- Eur. J."},{"key":"2026102007161022500_cit21","doi-asserted-by":"publisher","DOI":"10.1016\/j.bpc.2023.107022","article-title":"Recent advances\nin the modulation of amyloid protein aggregation using the supramolecular\nhost-guest approaches","volume":"297","author":"Maity","year":"2023","journal-title":"Biophys. Chem."},{"issue":"31","key":"2026102007161022500_cit22","doi-asserted-by":"publisher","first-page":"4041","DOI":"10.1002\/anie.200353565","article-title":"Inhibition of Amyloid\nFibril Formation by Peptide Analogues Modified\nwith \u03b1-Aminoisobutyric Acid","volume":"43","author":"Gilead","year":"2004","journal-title":"Angew. Chem.,\nInt. Ed."},{"issue":"37","key":"2026102007161022500_cit23","doi-asserted-by":"publisher","first-page":"11300","DOI":"10.1021\/ja072157y","article-title":"A Single-Point Mutation Converts\nthe Highly Amyloidogenic Human Islet Amyloid Polypeptide into a Potent\nFibrillization Inhibitor","volume":"129","author":"Abedini","year":"2007","journal-title":"J. Am. Chem. Soc."},{"issue":"9","key":"2026102007161022500_cit24","doi-asserted-by":"publisher","first-page":"3372","DOI":"10.1002\/anie.201906908","article-title":"Peptide-Based Molecular Strategies\nTo Interfere with Protein Misfolding, Aggregation, and Cell Degeneration","volume":"59","author":"Armiento","year":"2020","journal-title":"Angew. Chem., Int. Ed."},{"issue":"1","key":"2026102007161022500_cit25","doi-asserted-by":"publisher","first-page":"96","DOI":"10.1021\/acschembio.5c00685","article-title":"Probing the\nEffect of \u03b1-Helical Stapling Strategies on the Inhibition of\nPeptide Aggregation and Amyloid Cytotoxicity","volume":"21","author":"Babych","year":"2026","journal-title":"ACS Chem. Biol."},{"issue":"31","key":"2026102007161022500_cit26","doi-asserted-by":"publisher","first-page":"12837","DOI":"10.1002\/anie.202000148","article-title":"The Human Host-Defense Peptide Cathelicidin\nLL-37 is\na Nanomolar Inhibitor of Amyloid Self-Assembly of Islet Amyloid Polypeptide\n(IAPP)","volume":"59","author":"Armiento","year":"2020","journal-title":"Angew. Chem., Int. Ed."},{"key":"2026102007161022500_cit27","doi-asserted-by":"publisher","first-page":"124","DOI":"10.1016\/j.cbpa.2021.05.011","article-title":"Peptides for disrupting and degrading amyloids","volume":"64","author":"Liang","year":"2021","journal-title":"Curr. Opin. Chem. Biol."},{"issue":"8","key":"2026102007161022500_cit28","doi-asserted-by":"publisher","first-page":"1249","DOI":"10.1021\/acs.biochem.5c00634","article-title":"Prion Protein-Derived\nCell-Penetrating Peptide Inhibits Type II Diabetes-Associated Islet\nAmyloid Polypeptide Aggregation and Cytotoxicity","volume":"65","author":"Oh","year":"2026","journal-title":"Biochemistry"},{"issue":"3","key":"2026102007161022500_cit29","doi-asserted-by":"publisher","first-page":"339","DOI":"10.1006\/jmbi.2001.5244","article-title":"Structure-based design\nand study\nof non-amyloidogenic, double N-methylated IAPP amyloid core sequences\nas inhibitors of IAPP amyloid formation and cytotoxicity11Edited by\nR. Huber","volume":"315","author":"Kapurniotu","year":"2002","journal-title":"J. Mol. Biol."},{"issue":"7","key":"2026102007161022500_cit30","doi-asserted-by":"publisher","first-page":"2046","DOI":"10.1073\/pnas.0507471103","article-title":"Design of\na mimic of nonamyloidogenic and bioactive\nhuman islet amyloid polypeptide (IAPP) as nanomolar affinity inhibitor\nof IAPP cytotoxic fibrillogenesis","volume":"103","author":"Yan","year":"2006","journal-title":"Proc. Natl.\nAcad. Sci. U.S.A."},{"issue":"9","key":"2026102007161022500_cit31","doi-asserted-by":"publisher","first-page":"2522","DOI":"10.1002\/chem.201303928","article-title":"Synthesis of 2,5-Diaryl-Substituted\nThiophenes as Helical Mimetics: Towards the Modulation of Islet Amyloid\nPolypeptide (IAPP) Amyloid Fibril Formation and Cytotoxicity","volume":"20","author":"Hassanpour","year":"2014","journal-title":"Chem. - Eur. J."},{"issue":"4","key":"2026102007161022500_cit32","doi-asserted-by":"publisher","first-page":"225","DOI":"10.1039\/D0CB00086H","article-title":"Sub-stoichiometric\ninhibition of IAPP aggregation: a peptidomimetic approach to anti-amyloid\nagents","volume":"1","author":"Maity","year":"2020","journal-title":"RSC Chem. Biol."},{"issue":"9","key":"2026102007161022500_cit33","doi-asserted-by":"publisher","first-page":"943","DOI":"10.1016\/j.chembiol.2009.08.013","article-title":"A Peptidomimetic\nApproach to Targeting Pre-amyloidogenic States in Type II Diabetes","volume":"16","author":"Hebda","year":"2009","journal-title":"Chem. Biol."},{"issue":"4","key":"2026102007161022500_cit34","doi-asserted-by":"publisher","first-page":"736","DOI":"10.1002\/anie.200901694","article-title":"Synthetic \u03b1-Helix\nMimetics as Agonists and Antagonists\nof Islet Amyloid Polypeptide Aggregation","volume":"49","author":"Saraogi","year":"2010","journal-title":"Angew.\nChem., Int. Ed."},{"issue":"2","key":"2026102007161022500_cit35","doi-asserted-by":"publisher","DOI":"10.1002\/cmdc.202200499","article-title":"Inhibition\nof Amyloid Protein Aggregation Using Selected Peptidomimetics","volume":"18","author":"Maity","year":"2023","journal-title":"ChemMedChem"},{"issue":"1","key":"2026102007161022500_cit36","doi-asserted-by":"publisher","DOI":"10.1038\/srep40095","article-title":"Disaggregation\nof Amylin Aggregate by Novel Conformationally Restricted Aminobenzoic\nAcid containing \u03b1\/\u03b2 and \u03b1\/\u03b3 Hybrid Peptidomimetics","volume":"7","author":"Paul","year":"2017","journal-title":"Sci. Rep."},{"issue":"1","key":"2026102007161022500_cit37","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-018-03651-9","article-title":"Conformational switching\nwithin dynamic oligomers underpins toxic gain-of-function by diabetes-associated\namyloid","volume":"9","author":"Birol","year":"2018","journal-title":"Nat. Commun."},{"issue":"8","key":"2026102007161022500_cit38","doi-asserted-by":"publisher","DOI":"10.1016\/j.medj.2025.100771","article-title":"Alzheimer\u2019s\ndisease: Clinical trials to watch","volume":"6","author":"Sabbagh","year":"2025","journal-title":"Med"},{"issue":"32","key":"2026102007161022500_cit39","doi-asserted-by":"publisher","first-page":"16485","DOI":"10.1074\/jbc.R116.714576","article-title":"Cross-interactions\nbetween the Alzheimer Disease Amyloid-\u03b2\nPeptide and Other Amyloid Proteins: A Further Aspect of the Amyloid\nCascade Hypothesis*","volume":"291","author":"Luo","year":"2016","journal-title":"J. Biol. Chem."},{"issue":"46","key":"2026102007161022500_cit40","doi-asserted-by":"publisher","first-page":"7267","DOI":"10.1039\/C9TB01871A","article-title":"Fundamentals\nof cross-seeding of amyloid proteins: an introduction","volume":"7","author":"Ren","year":"2019","journal-title":"J. Mater. Chem. B"},{"issue":"1","key":"2026102007161022500_cit41","doi-asserted-by":"publisher","first-page":"47","DOI":"10.2174\/1567205043480555","article-title":"The Clinical\nand Biological Relationship between Type II Diabetes Mellitus and\nAlzheimers Disease","volume":"1","author":"Nicolls","year":"2004","journal-title":"Curr. Alzheimer Res."},{"issue":"2","key":"2026102007161022500_cit42","doi-asserted-by":"publisher","first-page":"384","DOI":"10.1016\/j.brainresrev.2007.09.001","article-title":"Common pathological\nprocesses in Alzheimer disease\nand type 2 diabetes: A review","volume":"56","author":"Li","year":"2007","journal-title":"Brain Res. Rev."},{"issue":"10","key":"2026102007161022500_cit43","doi-asserted-by":"publisher","first-page":"1759","DOI":"10.1021\/acschemneuro.5b00192","article-title":"Cross-Seeding\nInteraction between \u03b2-Amyloid and Human Islet Amyloid Polypeptide","volume":"6","author":"Hu","year":"2015","journal-title":"ACS Chem. Neurosci."},{"issue":"8","key":"2026102007161022500_cit44","doi-asserted-by":"publisher","first-page":"3086","DOI":"10.1021\/jacs.0c09967","article-title":"Peptidomimetic-Based\nVesicles Inhibit Amyloid-\u03b2 Fibrillation and Attenuate Cytotoxicity","volume":"143","author":"Maity","year":"2021","journal-title":"J. Am. Chem. Soc."},{"issue":"17","key":"2026102007161022500_cit45","doi-asserted-by":"publisher","first-page":"17490","DOI":"10.1074\/jbc.M311300200","article-title":"Seeding Specificity\nin Amyloid Growth Induced by Heterologous Fibrils*","volume":"279","author":"O\u2019Nuallain","year":"2004","journal-title":"J. Biol. Chem."},{"issue":"17","key":"2026102007161022500_cit46","doi-asserted-by":"publisher","first-page":"3081","DOI":"10.1002\/anie.200904902","article-title":"Identification\nof Hot Regions of the A\u03b2\u2013IAPP\nInteraction Interface as High-Affinity Binding Sites in both Cross-\nand Self-Association","volume":"49","author":"Andreetto","year":"2010","journal-title":"Angew. Chem., Int. Ed."},{"issue":"3","key":"2026102007161022500_cit47","doi-asserted-by":"publisher","first-page":"679","DOI":"10.1002\/anie.201105877","article-title":"Cross-Amyloid Interaction of A\u03b2 and IAPP at Lipid\nMembranes","volume":"51","author":"Seeliger","year":"2012","journal-title":"Angew. Chem., Int. Ed."},{"issue":"39","key":"2026102007161022500_cit48","doi-asserted-by":"publisher","first-page":"10378","DOI":"10.1002\/anie.201302840","article-title":"Selectively N-Methylated Soluble IAPP Mimics\nas Potent IAPP Receptor Agonists and Nanomolar Inhibitors of Cytotoxic\nSelf-Assembly of Both IAPP and A\u03b240","volume":"52","author":"Yan","year":"2013","journal-title":"Angew.\nChem., Int. Ed."},{"issue":"44","key":"2026102007161022500_cit49","doi-asserted-by":"publisher","first-page":"13095","DOI":"10.1002\/anie.201504973","article-title":"A Hot-Segment-Based\nApproach for the Design of Cross-Amyloid Interaction Surface Mimics\nas Inhibitors of Amyloid Self-Assembly","volume":"54","author":"Andreetto","year":"2015","journal-title":"Angew.\nChem., Int. Ed."},{"issue":"44","key":"2026102007161022500_cit50","doi-asserted-by":"publisher","first-page":"14503","DOI":"10.1002\/anie.201802979","article-title":"Designed Macrocyclic\nPeptides as Nanomolar Amyloid Inhibitors Based on Minimal Recognition\nElements","volume":"57","author":"Spanopoulou","year":"2018","journal-title":"Angew. Chem., Int. Ed."},{"issue":"14","key":"2026102007161022500_cit51","doi-asserted-by":"publisher","first-page":"5771","DOI":"10.1002\/anie.201914559","article-title":"Structural Insight into IAPP-Derived Amyloid\nInhibitors and Their Mechanism of Action","volume":"59","author":"Niu","year":"2020","journal-title":"Angew.\nChem., Int. Ed."},{"issue":"1","key":"2026102007161022500_cit52","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-022-32688-0","article-title":"Designed\npeptides as nanomolar cross-amyloid inhibitors acting via supramolecular\nnanofiber co-assembly","volume":"13","author":"Tas\u0327","year":"2022","journal-title":"Nat. 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