{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,22]],"date-time":"2026-07-22T05:02:47Z","timestamp":1784696567781,"version":"3.55.0"},"reference-count":65,"publisher":"MDPI AG","issue":"14","license":[{"start":{"date-parts":[[2026,7,20]],"date-time":"2026-07-20T00:00:00Z","timestamp":1784505600000},"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>Non-covalent forces are the primary drivers of biomolecular interactions. They also represent a key factor in the unexpected tendency for proteins, peptides, and even individual amino acids to self-assemble into precise supramolecular assemblies, often characterized by a \u03b2-rich, amyloid-like structure. Studies carried out in the last few decades have shown that peptides\/proteins self-assembly not only has structural consequences but also generates spectroscopic properties whose origin remains debated. Here, we investigated the spectroscopic properties of four peptides, GAIIGL, NNQQ, SSTSAA, and GNNQQNG (a derivative of the frequently studied GNNQQNY peptide), devoid of aromatic residues, whose crystallographic characterization has been seminal in elucidating the basis of the aggregation process. The spectroscopic behavior of these peptides was analyzed in two different media and in the solid state, highlighting the conditions that favor UV\u2013visible fluorescence emission. These investigations have also prompted the use of this fluorescence as a potential diagnostic tool in nanomedicine. Importantly, the identification of intrinsic fluorescence signatures in these amyloid-like assemblies may support the development of label-free optical approaches for the early detection and monitoring of aggregation-related pathological processes. For all peptides, the emitted fluorescence spans a rather wide range of wavelengths. Although centered in the blue region, a significant signal is also observed in the green region, independent of their physical state. The structural analysis of the solid used to collect the spectroscopic data reveals features related to the packings in the crystal state. This observation suggests that their three-dimensional crystal structures may serve as reliable models for studies aimed at correlating structural and spectroscopic features.<\/jats:p>","DOI":"10.3390\/ijms27146453","type":"journal-article","created":{"date-parts":[[2026,7,20]],"date-time":"2026-07-20T16:19:27Z","timestamp":1784564367000},"page":"6453","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["The Intrinsic UV\u2013Visible Fluorescence of Peptides Widely Used for Studying Amyloid Aggregation Devoid of Aromatic Residues"],"prefix":"10.3390","volume":"27","author":[{"ORCID":"https:\/\/orcid.org\/0009-0008-7060-6450","authenticated-orcid":false,"given":"Luca","family":"Cimmino","sequence":"first","affiliation":[{"name":"IRCCS SYNLAB SDN, Via Ferraris 144, 80146 Naples, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9273-0136","authenticated-orcid":false,"given":"Carlo","family":"Diaferia","sequence":"additional","affiliation":[{"name":"Department of Pharmacy, Research Centre on Bioactive Peptides (CIRPeB), University of Naples \u201cFederico II\u201d, Via De Amicis 95, 80145 Naples, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Erika","family":"Manicone","sequence":"additional","affiliation":[{"name":"Institute of Crystallography (IC), National Research Council (CNR), Via G. Amendola 122\/O, 70126 Bari, Italy"},{"name":"Department of Chemistry, University of Bari, Via E. Orabona 4, 70126 Bari, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2597-4883","authenticated-orcid":false,"given":"Davide","family":"Altamura","sequence":"additional","affiliation":[{"name":"Institute of Crystallography (IC), National Research Council (CNR), Via G. Amendola 122\/O, 70126 Bari, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Elisabetta","family":"Rosa","sequence":"additional","affiliation":[{"name":"IRCCS SYNLAB SDN, Via Ferraris 144, 80146 Naples, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0983-2885","authenticated-orcid":false,"given":"Cinzia","family":"Giannini","sequence":"additional","affiliation":[{"name":"Institute of Crystallography (IC), National Research Council (CNR), Via G. Amendola 122\/O, 70126 Bari, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3032-3375","authenticated-orcid":false,"given":"Luigi","family":"Vitagliano","sequence":"additional","affiliation":[{"name":"Institute of Biostructures and Bioimaging, National Research Council (CNR), Via Castellino 111, 80131 Naples, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7899-2359","authenticated-orcid":false,"given":"Antonella","family":"Accardo","sequence":"additional","affiliation":[{"name":"Department of Pharmacy, Research Centre on Bioactive Peptides (CIRPeB), University of Naples \u201cFederico II\u201d, Via De Amicis 95, 80145 Naples, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2026,7,20]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"5291","DOI":"10.1039\/b704781a","article-title":"Non-covalent interactions in biomacromolecules","volume":"9","author":"Hobza","year":"2007","journal-title":"Phys. Chem. Chem. Phys."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"4261","DOI":"10.1039\/D2CS00133K","article-title":"Noncovalent interactions in proteins and nucleic acids: Beyond hydrogen bonding and \u03c0-stacking","volume":"51","author":"Jena","year":"2022","journal-title":"Chem. Soc. Rev."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"5589","DOI":"10.1039\/C6CS00176A","article-title":"Peptide self-assembly: Thermodynamics and kinetics","volume":"45","author":"Wang","year":"2016","journal-title":"Chem. Soc. Rev."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1016\/bs.apcsb.2022.01.001","article-title":"Aromatic interactions directing peptide nano-assembly","volume":"130","author":"Sasidharan","year":"2022","journal-title":"Adv. Protein Chem. Struct. Biol."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"106769","DOI":"10.1016\/j.bpc.2022.106769","article-title":"Intrinsically disordered proteins\/regions and insight into their biomolecular interactions","volume":"283","author":"Chakrabarti","year":"2022","journal-title":"Biophys. Chem."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"55981","DOI":"10.1021\/acsami.5c15249","article-title":"Stimuli-responsive hydrogels from liquid\u2013liquid phase separations of FUS-derived peptides","volume":"17","author":"Rosa","year":"2025","journal-title":"ACS Appl. Mater. Interfaces"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"2756","DOI":"10.1039\/C6CS00004E","article-title":"Protein self-assembly via supramolecular strategies","volume":"45","author":"Bai","year":"2016","journal-title":"Chem. Soc. Rev."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"399","DOI":"10.2174\/1389557522666220819103907","article-title":"Peptide-based nanomaterials: Self-assembly and applications","volume":"23","author":"Tan","year":"2023","journal-title":"Mini Rev. Med. Chem."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"13105","DOI":"10.1021\/acs.jpcb.5c05756","article-title":"Investigating the role of pH and counterions in the intrinsic fluorescence of solid-state L-lysine","volume":"129","author":"Monti","year":"2025","journal-title":"J. Phys. Chem. B"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"9943","DOI":"10.1039\/C4CC04035J","article-title":"Self-assembly of NH2-(\u03b1,L-lysine)5-COOH and SDS into nanodiscs or nanoribbons regulated by pH","volume":"50","author":"Zhang","year":"2014","journal-title":"Chem. Commun."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"464","DOI":"10.1007\/s10930-024-10200-5","article-title":"Mechanism of peptide self-assembly and its study in biomedicine","volume":"43","author":"Yang","year":"2024","journal-title":"Protein J."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"4686","DOI":"10.1039\/D3SM00363A","article-title":"Self-assembled aggregates based on cationic amphiphilic peptides: Structural insight","volume":"19","author":"Rosa","year":"2023","journal-title":"Soft Matter"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"e2300171","DOI":"10.1002\/mabi.202300171","article-title":"Peptide-based optical\/electronic materials: Assembly and recent applications in biomedicine, sensing, and energy storage","volume":"23","author":"Tian","year":"2023","journal-title":"Macromol. Biosci."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"16196","DOI":"10.1021\/la303328p","article-title":"Effect of peptide and guest charge on the structural, mechanical and release properties of \u03b2-sheet forming peptides","volume":"28","author":"Roberts","year":"2012","journal-title":"Langmuir"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"773","DOI":"10.1038\/nature03680","article-title":"Structure of the cross-beta spine of amyloid-like fibrils","volume":"435","author":"Nelson","year":"2005","journal-title":"Nature"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1038\/nature05695","article-title":"Atomic structures of amyloid cross-beta spines reveal varied steric zippers","volume":"447","author":"Sawaya","year":"2007","journal-title":"Nature"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1042\/BCJ20240602","article-title":"Structural commonalities determined by physicochemical principles in the complex polymorphism of the amyloid state of proteins","volume":"482","author":"Errico","year":"2025","journal-title":"Biochem. J."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"22436","DOI":"10.1039\/D5NR02939B","article-title":"Structural and functional characterization of self-assembling fragments identified from the transthyretin amyloid-like structure","volume":"17","author":"Pizzella","year":"2025","journal-title":"Nanoscale"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"5473","DOI":"10.1039\/C9CS00199A","article-title":"Half a century of amyloids: Past, present and future","volume":"49","author":"Ke","year":"2020","journal-title":"Chem. Soc. Rev."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"041807","DOI":"10.1117\/1.NPh.3.4.041807","article-title":"Probing amyloid protein aggregation with optical superresolution methods: From the test tube to models of disease","volume":"3","author":"Kaminski","year":"2016","journal-title":"Neurophotonics"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"14039","DOI":"10.1002\/chem.201703055","article-title":"Structural Characterization of PEGylated Hexaphenylalanine Nanostructures Exhibiting Green Photoluminescence Emission","volume":"23","author":"Diaferia","year":"2017","journal-title":"Chem. Eur. J."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"18019","DOI":"10.1073\/pnas.0702843104","article-title":"Charge transport and intrinsic fluorescence in amyloid-like fibrils","volume":"104","author":"Pompa","year":"2007","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"3720","DOI":"10.1039\/D1CC01145F","article-title":"Amyloid-like Prep1 peptides exhibit reversible blue-green-red fluorescence in vitro and in living cells","volume":"57","author":"Monti","year":"2021","journal-title":"Chem. Commun."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"2156","DOI":"10.1039\/c3an36798c","article-title":"Protein amyloids develop an intrinsic fluorescence signature during aggregation","volume":"138","author":"Chan","year":"2013","journal-title":"Analyst"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"765","DOI":"10.1246\/bcsj.77.765","article-title":"Near Ultraviolet Absorption Arising from Lysine Residues in Close Proximity: A Probe to Monitor Protein Unfolding and Aggregation in Lysine-Rich Proteins","volume":"77","author":"Homchaudhuri","year":"2004","journal-title":"Bull. Chem. Soc. Jpn."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"e202400846","DOI":"10.1002\/chem.202400846","article-title":"The Characterization of Multifaceted PREP1 Peptides Provides Insights into Correlations between Spectroscopic and Structural Properties of Amyloid-like Assemblies","volume":"30","author":"Monti","year":"2024","journal-title":"Chem. Eur. J."},{"key":"ref_27","first-page":"645","article-title":"Self-assembly of a diphenylalanine-related dipeptide: The role of the C-terminal group","volume":"12","author":"Schiattarella","year":"2022","journal-title":"Sci. Rep."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"155","DOI":"10.3934\/biophy.2018.2.155","article-title":"Intrinsic blue-green fluorescence in amyloyd fibrils","volume":"5","author":"Sirangelo","year":"2018","journal-title":"AIMS Biophys."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"673","DOI":"10.1002\/cphc.201000996","article-title":"A FRET Sensor for Non-Invasive Imaging of Amyloid Formation In Vivo","volume":"12","author":"Bertoncini","year":"2011","journal-title":"ChemPhysChem"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"16733","DOI":"10.1039\/D5CP01547B","article-title":"Intrinsic visible emission of amyloid-\u03b2 oligomers: A potential tool for early alzheimer\u2019s diagnosis","volume":"27","author":"Novo","year":"2025","journal-title":"Phys. Chem. Chem. Phys."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"7106\u22127164","DOI":"10.1021\/acs.chemrev.3c00776","article-title":"Fluorescent Probes for Disease Diagnosis","volume":"124","author":"Wang","year":"2024","journal-title":"Chem. Rev."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"2249","DOI":"10.1016\/j.bios.2010.03.005","article-title":"Early detection of amyloid aggregation using intrinsic fluorescence","volume":"25","author":"Rolinski","year":"2010","journal-title":"Biosens. Bioelectron."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"3046","DOI":"10.1021\/jacs.5b11012","article-title":"Proton Transfer and Structure-Specific Fluorescence in Hydrogen Bond-Rich Protein Structures","volume":"138","author":"Pinotsi","year":"2016","journal-title":"J. Am. Chem. Soc."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"18042","DOI":"10.1021\/jacs.0c07134","article-title":"Toward Understanding Optical Properties of Amyloids: A Reaction Path and Nonadiabatic Dynamics Study","volume":"142","author":"Grisanti","year":"2020","journal-title":"J. Am. Chem. Soc."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"e2020389118","DOI":"10.1073\/pnas.2020389118","article-title":"Short hydrogen bonds enhance nonaromatic protein-related fluorescence","volume":"118","author":"Stephens","year":"2021","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_36","first-page":"6581","article-title":"Molecular Insights into the Intrinsic Fluorescence of Amyloid-like Aggregates","volume":"126","author":"Morzan","year":"2022","journal-title":"J. Phys. Chem. B"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"7325","DOI":"10.1038\/s41467-023-42874-3","article-title":"The carbonyl-lock mechanism underlying non-aromatic fluorescence in biological matter","volume":"14","author":"Semelak","year":"2023","journal-title":"Nat. Commun."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"e1703","DOI":"10.1002\/wcms.1703","article-title":"A brief history of amyloid aggregation simulations","volume":"14","author":"Fatafta","year":"2023","journal-title":"Wiley Interdiscip. Rev. Comput. Mol. Sci."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"11533","DOI":"10.1073\/pnas.0602345103","article-title":"Molecular dynamics analyses of cross-\u03b2-spine steric zipper models: \u03b2-sheet twisting and aggregation","volume":"103","author":"Esposito","year":"2006","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"16005","DOI":"10.1021\/ja075346p","article-title":"Thermodynamics and kinetics of aggregation for the GNNQQNY peptide","volume":"129","author":"Strodel","year":"2007","journal-title":"J. Am. Chem. Soc."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"1161","DOI":"10.1002\/bip.21182","article-title":"Dynamics and stability of amyloid-like steric zipper assemblies with hydrophobic dry interfaces","volume":"91","author":"Vitagliano","year":"2009","journal-title":"Biopolymers"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"5154","DOI":"10.1073\/pnas.0835307100","article-title":"The role of side-chain interactions in the early steps of aggregation: Molecular dynamics simulations of an amyloid-forming peptide from the yeast prion Sup35","volume":"100","author":"Gsponer","year":"2003","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"716","DOI":"10.1021\/acschemneuro.3c00754","article-title":"Molecular insights into the dynamics of amyloid fibril growth: Elongation and lateral assembly of GNNQQNY protofibrils","volume":"15","author":"John","year":"2024","journal-title":"ACS Chem. Neurosci."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"2208022","DOI":"10.1002\/adfm.202208022","article-title":"Dual-functional, multi-targeting GNNQQNY-AIE conjugates as amyloid probes and amyloid modulators via amyloid cross-seeding principle","volume":"32","author":"Tang","year":"2022","journal-title":"Adv. Funct. Mater."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"e70066","DOI":"10.1002\/pro.70066","article-title":"Guide to the structural characterization of protein aggregates and amyloid fibrils by CD spectroscopy","volume":"34","author":"Kardos","year":"2025","journal-title":"Protein Sci."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"1900","DOI":"10.1126\/science.1150057","article-title":"Role of Intermolecular Forces in Defining Material Properties of Protein Nanofibrils","volume":"318","author":"Knowles","year":"2007","journal-title":"Science"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"025101","DOI":"10.1063\/1.4732761","article-title":"Structural, thermodynamical, and dynamical properties of oligomers formed by the amyloid NNQQ peptide: Insights from coarse-grained simulations","volume":"137","author":"Lu","year":"2012","journal-title":"J. Chem. Phys."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"973","DOI":"10.1038\/nsmb.1643","article-title":"Molecular mechanisms for protein-encoded inheritance","volume":"16","author":"Wiltzius","year":"2009","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"627","DOI":"10.1016\/j.jmb.2009.09.056","article-title":"Binding modes of thioflavin-T to the single-layer beta-sheet of the peptide self-assembly mimics","volume":"394","author":"Wu","year":"2009","journal-title":"J. Mol. Biol."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1002\/bip.360370404","article-title":"The conformational analysis of peptides using Fourier transform IR spectroscopy","volume":"37","author":"Haris","year":"1995","journal-title":"Biopolymers"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"23931","DOI":"10.1039\/C9CP04648H","article-title":"Low energy optical excitations as an indicator of structural changes initiated at the termini of amyloid proteins","volume":"21","author":"Jong","year":"2019","journal-title":"Phys. Chem. Chem. Phys."},{"key":"ref_52","doi-asserted-by":"crossref","unstructured":"Biskupek, I., Czaplewski, C., Sawicka, J., I\u0142owska, E., Dzier\u017cy\u0144ska, M., Rodziewicz-Motowid\u0142o, S., and Liwo, A. (2022). Prediction of aggregation of biologically active peptides with the UNRES coarse-grained model. Biomolecules, 12.","DOI":"10.3390\/biom12081140"},{"key":"ref_53","doi-asserted-by":"crossref","unstructured":"Sza\u0142a-Mendyk, B., and Molski, A. (2020). Clustering and fibril formation during GNNQQNY aggregation: A molecular dynamics study. Biomolecules, 10.","DOI":"10.3390\/biom10101362"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"376","DOI":"10.1016\/j.jsb.2015.09.020","article-title":"Molecular events during the early stages of aggregation of GNNQQNY: An all-atom MD simulation study of randomly dispersed peptides","volume":"192","author":"Srivastava","year":"2015","journal-title":"J. Struct. Biol."},{"key":"ref_55","doi-asserted-by":"crossref","unstructured":"Nasica-Labouze, J., and Mousseau, N. (2012). Kinetics of amyloid aggregation: A study of the GNNQQNY prion sequence. PLoS Comput. Biol., 8.","DOI":"10.1371\/journal.pcbi.1002782"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"1036","DOI":"10.1016\/j.bbrc.2008.10.039","article-title":"Stability of single-sheet GNNQQNY aggregates analyzed by replica exchange molecular dynamics: Antiparallel versus parallel association","volume":"377","author":"Vitagliano","year":"2008","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"1965","DOI":"10.1529\/biophysj.108.129213","article-title":"Insights into stability and toxicity of amyloid-like oligomers by replica exchange molecular dynamics analyses","volume":"95","author":"Esposito","year":"2008","journal-title":"Biophys. J."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"1484","DOI":"10.1529\/biophysj.106.100537","article-title":"Molecular dynamics simulations on the oligomer-formation process of the GNNQQNY peptide from yeast prion protein Sup35","volume":"93","author":"Zhang","year":"2007","journal-title":"Biophys. J."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"824","DOI":"10.1529\/biophysj.106.083246","article-title":"Structural stability and dynamics of an amyloid-forming peptide GNNQQNY from the yeast prion Sup35","volume":"91","author":"Zheng","year":"2006","journal-title":"Biophys. J."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"2676","DOI":"10.1021\/acs.jpclett.6b00518","article-title":"Coarse master equations for binding kinetics of amyloid peptide dimers","volume":"7","author":"Leahy","year":"2016","journal-title":"J. Phys. Chem. Lett."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"165104","DOI":"10.1063\/1.3415372","article-title":"Relationship between population of the fibril-prone conformation in the monomeric state and oligomer formation times of peptides: Insights from all-atom simulations","volume":"132","author":"Nam","year":"2010","journal-title":"J. Chem. Phys."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"1469","DOI":"10.1002\/prot.24515","article-title":"Impact of sequence on the molecular assembly of short amyloid peptides","volume":"82","author":"Wagoner","year":"2014","journal-title":"Proteins"},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"578","DOI":"10.1002\/bip.21405","article-title":"Insight into the stability of cross-\u03b2 amyloid fibril from molecular dynamics simulation","volume":"93","author":"Chen","year":"2010","journal-title":"Biopolymers"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"869","DOI":"10.1107\/S0021889812025733","article-title":"X-ray microimaging laboratory (XMI-LAB)","volume":"45","author":"Altamura","year":"2012","journal-title":"J. Appl. Crystallogr."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"1817","DOI":"10.1107\/S1600576725005904","article-title":"SUNBIM 4.0 software: New developments in small- and wide-angle X-ray scattering data analysis for scanning mode and grazing-incidence geometry","volume":"58","author":"Scattarella","year":"2025","journal-title":"J. Appl. Crystallogr."}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/27\/14\/6453\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,7,22]],"date-time":"2026-07-22T04:16:10Z","timestamp":1784693770000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/27\/14\/6453"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,7,20]]},"references-count":65,"journal-issue":{"issue":"14","published-online":{"date-parts":[[2026,7]]}},"alternative-id":["ijms27146453"],"URL":"https:\/\/doi.org\/10.3390\/ijms27146453","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,7,20]]}}}