{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,23]],"date-time":"2026-10-23T07:23:56Z","timestamp":1792740236806,"version":"4.5.0"},"reference-count":56,"publisher":"American Chemical Society (ACS)","issue":"9","license":[{"start":{"date-parts":[[2017,8,14]],"date-time":"2017-08-14T00:00:00Z","timestamp":1502668800000},"content-version":"vor","delay-in-days":11,"URL":"https:\/\/pubs.acs.org\/page\/policy\/authorchoice_ccby_termsofuse.html"}],"funder":[{"DOI":"10.13039\/100010665","name":"H2020 Marie Sklodowska-Curie Actions","doi-asserted-by":"publisher","award":["701664"],"award-info":[{"award-number":["701664"]}],"id":[{"id":"10.13039\/100010665","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100011199","name":"FP7 Ideas: European Research Council","doi-asserted-by":"publisher","award":["616417"],"award-info":[{"award-number":["616417"]}],"id":[{"id":"10.13039\/100011199","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100011264","name":"FP7 People: Marie-Curie Actions","doi-asserted-by":"publisher","award":["623123"],"award-info":[{"award-number":["623123"]}],"id":[{"id":"10.13039\/100011264","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000266","name":"Engineering and Physical Sciences Research Council","doi-asserted-by":"publisher","award":["EP\/K020641\/1"],"award-info":[{"award-number":["EP\/K020641\/1"]}],"id":[{"id":"10.13039\/501100000266","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000266","name":"Engineering and Physical Sciences Research Council","doi-asserted-by":"publisher","award":["EP\/K031953\/1"],"award-info":[{"award-number":["EP\/K031953\/1"]}],"id":[{"id":"10.13039\/501100000266","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000943","name":"Commonwealth Scientific and Industrial Research Organisation","doi-asserted-by":"publisher","award":["NA"],"award-info":[{"award-number":["NA"]}],"id":[{"id":"10.13039\/501100000943","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/na","name":"Taiwan Strategic Alliance","doi-asserted-by":"publisher","award":["UK-ICL-102-S03"],"award-info":[{"award-number":["UK-ICL-102-S03"]}],"id":[{"id":"10.13039\/na","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2017,9,26]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Determining the structural origins of amyloid fibrillation is essential for understanding both the pathology of amyloidosis and the rational design of inhibitors to prevent or reverse amyloid formation. In this work, the decisive roles of peptide structures on amyloid self-assembly and morphological diversity were investigated by the design of eight amyloidogenic peptides derived from islet amyloid polypeptide. Among the segments, two distinct morphologies were highlighted in the form of twisted and planar (untwisted) ribbons with varied diameters, thicknesses, and lengths. In particular, transformation of amyloid fibrils from twisted ribbons into untwisted structures was triggered by substitution of the C-terminal serine with threonine, where the side chain methyl group was responsible for the distinct morphological change. This effect was confirmed following serine substitution with alanine and valine and was ascribed to the restriction of intersheet torsional strain through the increased hydrophobic interactions and hydrogen bonding. We also studied the variation of fibril morphology (i.e., association and helicity) and peptide aggregation propensity by increasing the hydrophobicity of the peptide side group, capping the N-terminus, and extending sequence length. We anticipate that our insights into sequence-dependent fibrillation and morphological diversity will shed light on the structural interpretation of amyloidogenesis and development of structure-specific imaging agents and aggregation inhibitors.<\/jats:p>","DOI":"10.1021\/acsnano.7b02325","type":"journal-article","created":{"date-parts":[[2017,8,3]],"date-time":"2017-08-03T15:34:31Z","timestamp":1501774471000},"page":"8579-8589","source":"Crossref","is-referenced-by-count":60,"title":["Sequence-Dependent Self-Assembly and Structural Diversity\nof Islet Amyloid Polypeptide-Derived \u03b2-Sheet Fibrils"],"prefix":"10.1021","volume":"11","author":[{"given":"Shih-Ting","family":"Wang","sequence":"first","affiliation":[{"name":"Imperial College London , , Exhibition Road , ,","place":["London, United Kingdom, SW7 2AZ"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yiyang","family":"Lin","sequence":"additional","affiliation":[{"name":"Imperial College London , , Exhibition Road , ,","place":["London, United Kingdom, SW7 2AZ"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ryan K.","family":"Spencer","sequence":"additional","affiliation":[{"name":"Lawrence Berkeley National Laboratory , , 1 Cyclotron Road , , ,","place":["Berkeley, California, United States, 94720"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7795-9648","authenticated-orcid":true,"given":"Michael R.","family":"Thomas","sequence":"additional","affiliation":[{"name":"Imperial College London , , Exhibition Road , ,","place":["London, United Kingdom, SW7 2AZ"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4137-6453","authenticated-orcid":true,"given":"Andy I.","family":"Nguyen","sequence":"additional","affiliation":[{"name":"Lawrence Berkeley National Laboratory , , 1 Cyclotron Road , , ,","place":["Berkeley, California, United States, 94720"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nadav","family":"Amdursky","sequence":"additional","affiliation":[{"name":"Imperial College London , , Exhibition Road , ,","place":["London, United Kingdom, SW7 2AZ"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2881-4965","authenticated-orcid":true,"given":"E. Thomas","family":"Pashuck","sequence":"additional","affiliation":[{"name":"Imperial College London , , Exhibition Road , ,","place":["London, United Kingdom, SW7 2AZ"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stacey C.","family":"Skaalure","sequence":"additional","affiliation":[{"name":"Imperial College London , , Exhibition Road , ,","place":["London, United Kingdom, SW7 2AZ"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Cheng Yu","family":"Song","sequence":"additional","affiliation":[{"name":"Lawrence Berkeley National Laboratory , , 1 Cyclotron Road , , ,","place":["Berkeley, California, United States, 94720"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Paresh A.","family":"Parmar","sequence":"additional","affiliation":[{"name":"Imperial College London , , Exhibition Road , ,","place":["London, United Kingdom, SW7 2AZ"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rhodri M.","family":"Morgan","sequence":"additional","affiliation":[{"name":"Imperial College London , , Exhibition Road , ,","place":["London, United Kingdom, SW7 2AZ"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Peter","family":"Ercius","sequence":"additional","affiliation":[{"name":"Lawrence Berkeley National Laboratory , , 1 Cyclotron Road , , ,","place":["Berkeley, California, United States, 94720"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shaul","family":"Aloni","sequence":"additional","affiliation":[{"name":"Lawrence Berkeley National Laboratory , , 1 Cyclotron Road , , ,","place":["Berkeley, California, United States, 94720"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3055-8860","authenticated-orcid":true,"given":"Ronald N.","family":"Zuckermann","sequence":"additional","affiliation":[{"name":"Lawrence Berkeley National Laboratory , , 1 Cyclotron Road , , ,","place":["Berkeley, California, United States, 94720"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7335-266X","authenticated-orcid":true,"given":"Molly M.","family":"Stevens","sequence":"additional","affiliation":[{"name":"Imperial College London , , Exhibition Road , ,","place":["London, United Kingdom, SW7 2AZ"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2017,8,3]]},"reference":[{"key":"2026090222251526100_cit1","doi-asserted-by":"publisher","first-page":"329","DOI":"10.1016\/S0968-0004(99)01445-0","article-title":"Protein\nMisfolding, Evolution and Disease","volume":"24","author":"Dobson","year":"1999","journal-title":"Trends Biochem.\nSci."},{"key":"2026090222251526100_cit2","doi-asserted-by":"publisher","first-page":"60","DOI":"10.1016\/S0959-440X(99)00049-4","article-title":"Amyloid Fibrillogenesis: Themes and\nVariations","volume":"10","author":"Rochet","year":"2000","journal-title":"Curr. Opin. Struct. Biol."},{"key":"2026090222251526100_cit3","doi-asserted-by":"publisher","first-page":"712","DOI":"10.1126\/science.174.4010.712","article-title":"Creation\nof \u2033Amyloid\u2033 Fibrils from Bence Jones Proteins","volume":"174","author":"Glenner","year":"1971","journal-title":"Science"},{"key":"2026090222251526100_cit4","doi-asserted-by":"publisher","first-page":"343","DOI":"10.1016\/0022-2836(68)90014-4","article-title":"\u2033Cross-Beta\u2033\nConformation in Proteins","volume":"32","author":"Geddes","year":"1968","journal-title":"J. Mol. Biol."},{"key":"2026090222251526100_cit5","doi-asserted-by":"publisher","first-page":"773","DOI":"10.1038\/nature03680","article-title":"Structure\nof the Cross-\u03b2 Spine of Amyloid-Like Fibrils","volume":"435","author":"Nelson","year":"2005","journal-title":"Nature"},{"key":"2026090222251526100_cit6","doi-asserted-by":"publisher","first-page":"3590","DOI":"10.1073\/pnas.96.7.3590","article-title":"Designing Conditions for in Vitro Formation of Amyloid Protofilaments and Fibrils","volume":"96","author":"Chiti","year":"1999","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"2026090222251526100_cit7","doi-asserted-by":"publisher","first-page":"5147","DOI":"10.1021\/cr3000994","article-title":"The Amyloid\nBeta Peptide: A Chemist\u2019s Perspective. Role in Alzheimer\u2019s\nand Fibrillization","volume":"112","author":"Hamley","year":"2012","journal-title":"Chem. Rev."},{"key":"2026090222251526100_cit8","doi-asserted-by":"publisher","first-page":"262","DOI":"10.1126\/science.1105850","article-title":"Self-Propagating, Molecular-Level\nPolymorphism in Alzheimer\u2019s\n\u03b2-Amyloid Fibrils","volume":"307","author":"Petkova","year":"2005","journal-title":"Science"},{"key":"2026090222251526100_cit9","doi-asserted-by":"publisher","first-page":"6881","DOI":"10.1039\/C4CS00164H","article-title":"The Physical Properties\nof Supramolecular Peptide Assemblies: From\nBuilding Block Association to Technological Applications","volume":"43","author":"Adler-Abramovich","year":"2014","journal-title":"Chem. Soc. Rev."},{"key":"2026090222251526100_cit10","doi-asserted-by":"publisher","first-page":"8128","DOI":"10.1002\/anie.200700861","article-title":"Peptide\nFibrillization","volume":"46","author":"Hamley","year":"2007","journal-title":"Angew. Chem., Int. Ed."},{"key":"2026090222251526100_cit11","doi-asserted-by":"publisher","first-page":"32","DOI":"10.4161\/pri.1.1.4095","article-title":"Self Assembly\nof Short Aromatic Peptides into Amyloid Fibrils and Related Nanostructures","volume":"1","author":"Gazit","year":"2007","journal-title":"Prion"},{"key":"2026090222251526100_cit12","doi-asserted-by":"publisher","first-page":"880","DOI":"10.1021\/acsnano.5b06011","article-title":"Electrostatic-Driven\nLamination and Untwisting of \u03b2-Sheet Assemblies","volume":"10","author":"Hu","year":"2016","journal-title":"ACS Nano"},{"key":"2026090222251526100_cit13","doi-asserted-by":"publisher","first-page":"1900","DOI":"10.1126\/science.1150057","article-title":"Role of Intermolecular Forces in\nDefining Material Properties of Protein Nanofibrils","volume":"318","author":"Knowles","year":"2007","journal-title":"Science"},{"key":"2026090222251526100_cit14","doi-asserted-by":"publisher","first-page":"16052","DOI":"10.1073\/pnas.252340199","article-title":"De Novo Designed Peptide-Based Amyloid Fibrils","volume":"99","author":"Lo\u0301pez de la Paz","year":"2002","journal-title":"Proc.\nNatl. Acad. Sci. U. S. A."},{"key":"2026090222251526100_cit15","doi-asserted-by":"publisher","first-page":"87","DOI":"10.1073\/pnas.2634884100","article-title":"Sequence Determinants of Amyloid\nFibril Formation","volume":"101","author":"Lo\u0301pez de la Paz","year":"2004","journal-title":"Proc. Natl. Acad. Sci. U.\nS. A."},{"key":"2026090222251526100_cit16","doi-asserted-by":"publisher","first-page":"7574","DOI":"10.1038\/ncomms8574","article-title":"Supramolecular Amplification of Amyloid Self-Assembly\nby Iodination","volume":"6","author":"Bertolani","year":"2015","journal-title":"Nat. Commun."},{"key":"2026090222251526100_cit17","doi-asserted-by":"publisher","first-page":"2317","DOI":"10.1002\/anie.200805500","article-title":"Helical-Ribbon Formation\nby a Beta-Amino Acid Modified Amyloid \u03b2-Peptide Fragment","volume":"48","author":"Castelletto","year":"2009","journal-title":"Angew. Chem., Int. Ed."},{"key":"2026090222251526100_cit18","doi-asserted-by":"publisher","first-page":"6391","DOI":"10.1021\/ja0341642","article-title":"Exploiting Amyloid Fibril Lamination for Nanotube Self-Assembly","volume":"125","author":"Lu","year":"2003","journal-title":"J. Am. Chem. Soc."},{"key":"2026090222251526100_cit19","doi-asserted-by":"publisher","first-page":"3491","DOI":"10.1021\/bi991527v","article-title":"Two-Dimensional\nStructure of \u03b2-Amyloid(10\u201335) Fibrils","volume":"39","author":"Benzinger","year":"2000","journal-title":"Biochemistry"},{"key":"2026090222251526100_cit20","doi-asserted-by":"publisher","first-page":"10018","DOI":"10.1021\/bi801081c","article-title":"Cross-Strand Pairing and Amyloid Assembly","volume":"47","author":"Liang","year":"2008","journal-title":"Biochemistry"},{"key":"2026090222251526100_cit21","doi-asserted-by":"publisher","first-page":"5556","DOI":"10.1021\/ja301642c","article-title":"Coassembly of Enantiomeric\nAmphipathic Peptides into Amyloid-Inspired Rippled \u03b2-Sheet Fibrils","volume":"134","author":"Swanekamp","year":"2012","journal-title":"J. Am. Chem. Soc."},{"key":"2026090222251526100_cit22","doi-asserted-by":"publisher","first-page":"12461","DOI":"10.1021\/ja507051w","article-title":"Amino Acid Sequence\nin Constitutionally Isomeric Tetrapeptide Amphiphiles Dictates Architecture\nof One-Dimensional Nanostructures","volume":"136","author":"Cui","year":"2014","journal-title":"J. Am. Chem.\nSoc."},{"key":"2026090222251526100_cit23","doi-asserted-by":"publisher","first-page":"761","DOI":"10.1110\/ps.062609607","article-title":"Cooperative Hydrogen\nBonding in Amyloid Formation","volume":"16","author":"Tsemekhman","year":"2007","journal-title":"Protein Sci."},{"key":"2026090222251526100_cit24","doi-asserted-by":"publisher","first-page":"1053","DOI":"10.1002\/prot.24007","article-title":"Role of Amino Acid\nHydrophobicity, Aromaticity, and Molecular Volume on Iapp(20\u201329)\nAmyloid Self-Assembly","volume":"80","author":"Doran","year":"2012","journal-title":"Proteins: Struct., Funct.,\nGenet."},{"key":"2026090222251526100_cit25","doi-asserted-by":"publisher","first-page":"6506","DOI":"10.1021\/acs.langmuir.6b00704","article-title":"Supramolecular\nNanostructure Formation of Coassembled\nAmyloid Inspired Peptides","volume":"32","author":"Cinar","year":"2016","journal-title":"Langmuir"},{"key":"2026090222251526100_cit26","doi-asserted-by":"publisher","first-page":"519","DOI":"10.1073\/pnas.1217742110","article-title":"Aliphatic Peptides\nShow Similar Self-Assembly\nto Amyloid Core Sequences, Challenging the Importance of Aromatic\nInteractions in Amyloidosis","volume":"110","author":"Lakshmanan","year":"2013","journal-title":"Proc. Natl. Acad.\nSci. U. S. A."},{"key":"2026090222251526100_cit27","doi-asserted-by":"publisher","first-page":"2079","DOI":"10.1126\/science.274.5295.2079","article-title":"Evidence for the Conformation of the Pathologic Isoform\nof the Prion Protein Enciphering and Propagating Prion Diversity","volume":"274","author":"Telling","year":"1996","journal-title":"Science"},{"key":"2026090222251526100_cit28","doi-asserted-by":"crossref","first-page":"17243","DOI":"10.1016\/S0021-9258(19)77825-9","article-title":"An Islet Amyloid Peptide Is Derived from an 89-Amino\nAcid Precursor by Proteolytic Processing","volume":"263","author":"Sanke","year":"1988","journal-title":"J.\nBiol. Chem."},{"key":"2026090222251526100_cit29","doi-asserted-by":"publisher","first-page":"608","DOI":"10.1016\/S0006-291X(88)80538-2","article-title":"Amyloid Fibrils Formed from a Segment\nof the Pancreatic Islet Amyloid Protein","volume":"155","author":"Glenner","year":"1988","journal-title":"Biochem.\nBiophys. Res. Commun."},{"key":"2026090222251526100_cit30","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."},{"key":"2026090222251526100_cit31","doi-asserted-by":"publisher","first-page":"1467","DOI":"10.1110\/ps.036509.108","article-title":"Atomic Structure of the Cross-\u03b2\nSpine of Islet Amyloid Polypeptide (Amylin)","volume":"17","author":"Wiltzius","year":"2008","journal-title":"Protein Sci."},{"key":"2026090222251526100_cit32","doi-asserted-by":"publisher","first-page":"17","DOI":"10.1006\/jsbi.1997.3858","article-title":"Polymorphic Fibrillar Assembly of Human Amylin","volume":"119","author":"Goldsbury","year":"1997","journal-title":"J. Struct. Biol."},{"key":"2026090222251526100_cit33","doi-asserted-by":"publisher","first-page":"11857","DOI":"10.1073\/pnas.191250198","article-title":"Hierarchical Self-Assembly\nof Chiral Rod-Like Molecules as a Model for Peptide \u03b2-Sheet\nTapes, Ribbons, Fibrils, and Fibers","volume":"98","author":"Aggeli","year":"2001","journal-title":"Proc. Natl.\nAcad. Sci. U. S. A."},{"key":"2026090222251526100_cit34","doi-asserted-by":"publisher","first-page":"9619","DOI":"10.1021\/ja021047i","article-title":"Ph as a Trigger\nof Peptide \u03b2-Sheet Self-Assembly and Reversible Switching between\nNematic and Isotropic Phases","volume":"125","author":"Aggeli","year":"2003","journal-title":"J. Am. Chem. Soc."},{"key":"2026090222251526100_cit35","doi-asserted-by":"publisher","first-page":"727","DOI":"10.1038\/nmat4598","article-title":"Morphology Selection Via Geometric\nFrustration in Chiral Filament Bundles","volume":"15","author":"Hall","year":"2016","journal-title":"Nat.\nMater."},{"key":"2026090222251526100_cit36","doi-asserted-by":"publisher","first-page":"2946","DOI":"10.1021\/ja711213s","article-title":"Quadruple\nHelix Formation of a Photoresponsive Peptide\nAmphiphile and Its Light-Triggered Dissociation into Single Fibers","volume":"130","author":"Muraoka","year":"2008","journal-title":"J. Am. Chem. Soc."},{"key":"2026090222251526100_cit37","doi-asserted-by":"publisher","first-page":"8819","DOI":"10.1021\/ja100613w","article-title":"Direct Observation of Morphological Tranformation from\nTwisted Ribbons into Helical Ribbons","volume":"132","author":"Pashuck","year":"2010","journal-title":"J. Am.\nChem. Soc."},{"key":"2026090222251526100_cit38","doi-asserted-by":"publisher","first-page":"5591","DOI":"10.1073\/pnas.042681399","article-title":"Amyloid Fibers Are\nWater-Filled Nanotubes","volume":"99","author":"Perutz","year":"2002","journal-title":"Proc. Natl. Acad. Sci.\nU. S. A."},{"key":"2026090222251526100_cit39","doi-asserted-by":"publisher","first-page":"3784","DOI":"10.1016\/j.chroma.2009.02.046","article-title":"Mechanistic Studies on the Chiral\nRecognition of Polysaccharide-Based\nChiral Stationary Phases Using Liquid Chromatography and Vibrational\nCircular Dichroism: Reversal of Elution Order of N-Substituted Alpha-Methyl\nPhenylalanine Esters","volume":"1216","author":"Ma","year":"2009","journal-title":"J. Chromatogr. A"},{"key":"2026090222251526100_cit40","volume-title":"The CH\/\u03a0 Interaction:\nEvidence, Nature, and Consequences","author":"Nishio","year":"1998"},{"key":"2026090222251526100_cit41","doi-asserted-by":"publisher","first-page":"787","DOI":"10.1002\/bip.20294","article-title":"Peptide Hairpins with Strand Segments Containing \u03b1-\nand \u03b2-Amino Acid Residues: Cross-Strand Aromatic Interactions\nof Facing Phe Residues","volume":"80","author":"Roy","year":"2005","journal-title":"Biopolymers"},{"key":"2026090222251526100_cit42","doi-asserted-by":"publisher","first-page":"9978","DOI":"10.1021\/jp902860a","article-title":"Influence\nof the Solvent on the Self-Assembly of a Modified Amyloid Beta Peptide\nFragment. I. Morphological Investigation","volume":"113","author":"Castelletto","year":"2009","journal-title":"J.\nPhys. Chem. B"},{"key":"2026090222251526100_cit43","doi-asserted-by":"publisher","first-page":"341","DOI":"10.3233\/BSI-150123","article-title":"Investigation of Neurodegenerative\nDiseases from Body Fluid Samples Using Fourier Transform Infrared\nSpectroscopy","volume":"4","author":"Sevinc","year":"2015","journal-title":"Biomed. Spectrosc. Imaging"},{"key":"2026090222251526100_cit44","doi-asserted-by":"publisher","first-page":"14990","DOI":"10.1021\/ja802483d","article-title":"Structural\nInsights into the Polymorphism of Amyloid-Like\nFibrils Formed by Region 20\u201329 of Amylin Revealed by Solid-State\nNmr and X-Ray Fiber Diffraction","volume":"130","author":"Madine","year":"2008","journal-title":"J. Am. Chem.\nSoc."},{"key":"2026090222251526100_cit45","doi-asserted-by":"publisher","first-page":"19285","DOI":"10.1073\/pnas.1314481110","article-title":"Mechanism\nof Iapp Amyloid Fibril Formation Involves an Intermediate with a Transient\n\u03b2-Sheet","volume":"110","author":"Buchanan","year":"2013","journal-title":"Proc. Natl. Acad. Sci. U. S.\nA."},{"key":"2026090222251526100_cit46","doi-asserted-by":"publisher","first-page":"5810","DOI":"10.1021\/acs.jpcb.5b09981","article-title":"Crystal Structures\nof Iapp Amyloidogenic Segments Reveal a Novel Packing Motif of out-of-Register\nBeta Sheets","volume":"120","author":"Soriaga","year":"2016","journal-title":"J. Phys. Chem. B"},{"key":"2026090222251526100_cit47","doi-asserted-by":"publisher","first-page":"9458","DOI":"10.1021\/ja072181b","article-title":"Serine Versus Threonine\nGlycosylation:\nThe Methyl Group Causes a Drastic Alteration on the Carbohydrate Orientation\nand on the Surrounding Water Shell","volume":"129","author":"Corzana","year":"2007","journal-title":"J. Am. Chem.\nSoc."},{"key":"2026090222251526100_cit48","doi-asserted-by":"publisher","first-page":"874","DOI":"10.1002\/ange.200353110","article-title":"Antifreeze\nGlycoproteins: Elucidation of the Structural\nMotifs That Are Essential for Antifreeze Activity","volume":"116","author":"Tachibana","year":"2004","journal-title":"Angew. Chem."},{"key":"2026090222251526100_cit49","doi-asserted-by":"publisher","first-page":"2004","DOI":"10.1021\/bm500075r","article-title":"Sequence\nEffects of Self-Assembling Multidomain Peptide Hydrogels on Encapsulated\nShed Cells","volume":"15","author":"Kang","year":"2014","journal-title":"Biomacromolecules"},{"key":"2026090222251526100_cit50","doi-asserted-by":"publisher","first-page":"9830","DOI":"10.1002\/anie.201502813","article-title":"Deciphering the Non-Equivalence of Serine and Threonine\nO-Glycosylation Points: Implications for Molecular Recognition of\nthe Tn Antigen by an Anti-Muc1 Antibody","volume":"54","author":"Marti\u0301nez-Sa\u0301ez","year":"2015","journal-title":"Angew.\nChem., Int. Ed."},{"key":"2026090222251526100_cit51","doi-asserted-by":"publisher","first-page":"109","DOI":"10.1039\/fs9821700109","article-title":"Hydrophobic Moments\nand Protein Structure. Faraday Symp","volume":"17","author":"Eisenberg","year":"1982","journal-title":"Faraday Symp. Chem. Soc."},{"key":"2026090222251526100_cit52","doi-asserted-by":"publisher","first-page":"659","DOI":"10.1016\/0022-2836(87)90189-6","article-title":"Hydrophobicity Scales\nand Computational Techniques\nfor Detecting Amphipathic Structures in Proteins","volume":"195","author":"Cornette","year":"1987","journal-title":"J. Mol. Biol."},{"key":"2026090222251526100_cit53","doi-asserted-by":"publisher","first-page":"125","DOI":"10.1016\/0022-2836(84)90309-7","article-title":"Analysis of\nMembrane\nand Surface Protein Sequences with the Hydrophobic Moment Plot","volume":"179","author":"Eisenberg","year":"1984","journal-title":"J. Mol. Biol."},{"key":"2026090222251526100_cit54","doi-asserted-by":"publisher","first-page":"217","DOI":"10.1016\/S0065-3233(06)73007-8","article-title":"From the Polymorphism of Amyloid\nFibrils to Their Assembly Mechanism\nand Cytotoxicity","volume":"73","author":"Kreplak","year":"2006","journal-title":"Adv. Protein Chem."},{"key":"2026090222251526100_cit55","doi-asserted-by":"publisher","first-page":"59","DOI":"10.1006\/jsbi.1997.3859","article-title":"The Toxicity\nof the Alzheimer\u2019s\n\u03b2-Amyloid Peptide Correlates with a Distinct Fiber Morphology","volume":"119","author":"Seilheimer","year":"1997","journal-title":"J. Struct. Biol."},{"key":"2026090222251526100_cit56","doi-asserted-by":"publisher","first-page":"324","DOI":"10.1107\/S0021889812004037","article-title":"Nika: Software\nfor Two-Dimensional Data Reduction","volume":"45","author":"Ilavsky","year":"2012","journal-title":"J. Appl.\nCrystallogr."}],"container-title":["ACS Nano"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/acsnano.7b02325","content-type":"application\/pdf","content-version":"vor","intended-application":"unspecified"},{"URL":"https:\/\/pubs.acs.org\/ancac3\/article-pdf\/11\/9\/8579\/67097837\/acsnano.7b02325.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/pubs.acs.org\/ancac3\/article-pdf\/11\/9\/8579\/67097837\/acsnano.7b02325.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,9,3]],"date-time":"2026-09-03T02:25:25Z","timestamp":1788402325000},"score":1,"resource":{"primary":{"URL":"https:\/\/pubs.acs.org\/ancac3\/article\/11\/9\/8579\/744219\/Sequence-Dependent-Self-Assembly-and-Structural"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2017,8,3]]},"references-count":56,"journal-issue":{"issue":"9","published-online":{"date-parts":[[2017,8,3]]},"published-print":{"date-parts":[[2017,9,26]]}},"URL":"https:\/\/doi.org\/10.1021\/acsnano.7b02325","relation":{},"ISSN":["1936-0851","1936-086X"],"issn-type":[{"value":"1936-0851","type":"print"},{"value":"1936-086X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2017,8,3]]}}}