{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,23]],"date-time":"2026-10-23T19:45:29Z","timestamp":1792784729515,"version":"4.5.0"},"reference-count":103,"publisher":"American Chemical Society (ACS)","issue":"41","license":[{"start":{"date-parts":[[2026,10,2]],"date-time":"2026-10-02T00:00:00Z","timestamp":1790899200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"funder":[{"name":"European Commission (Horizon Europe Framework Programme)","award":["Smart Response Self-Disinfected Biobased Nanocoate"],"award-info":[{"award-number":["Smart Response Self-Disinfected Biobased Nanocoate"]}],"id":[{"id":"https:\/\/ror.org\/00k4n6c32","id-type":"ROR","asserted-by":"crossref"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,10,15]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Keratin-derived antimicrobial peptides (KAMPs) from human corneal epithelial cells have received considerable attention due to their biocidal activity against both Gram-positive and Gram-negative bacteria without possessing the conventional characteristics of known antimicrobial peptides (AMPs), such as ordered secondary structure elements and a net positive charge. Here, we perform unbiased, all-atom molecular dynamics (MD) simulations for seven members of the glycine-rich KAMP family and for Pw-Antibac123, which is a distinct keratin-derived peptide obtained through chicken feather hydrolyzates. This study first aims to investigate the structural dynamics of these peptides in dilute and semidilute aqueous solutions. Our results verify the noncanonical structure of KAMPs and validate the molecular model of Pw-Antibac123 that has been proposed in the literature. Increasing the peptide concentration in the aqueous solution leads to self-assembly and peptide aggregation, due to the development of interpeptide hydrogen bonds and the strong effect of electrostatic interactions. The effect of intermolecular amino acid interactions on the secondary structure of KAMPs is also discussed, allowing us to identify strong synergies between specific amino acid pairs, such as serine and glycine, valine and leucine, and arginine and isoleucine. Subsequently, we focus on how KAMP-18C, an 18-residue-long KAMP, interacts with model Gram-positive lipid bilayers. Since spontaneous aggregation is not observed, we construct artificial pores and embed peptides within the membrane to assess the stability of these systems. We discuss how our findings correlate with proposed mechanisms of action for AMPs.<\/jats:p>","DOI":"10.1021\/acs.jpcb.6c04420","type":"journal-article","created":{"date-parts":[[2026,10,2]],"date-time":"2026-10-02T17:01:37Z","timestamp":1790960497000},"page":"10941-10960","source":"Crossref","is-referenced-by-count":0,"title":["Conformational,\nAggregation, and Membrane Interaction\nDynamics of Keratin-Derived Antimicrobial Peptides from Molecular\nDynamics Simulations"],"prefix":"10.1021","volume":"130","author":[{"given":"Panagiotis","family":"Panagopoulos Papageorgiou","sequence":"first","affiliation":[{"name":"University of Patras , , ,","place":["Patras, Greece, GR 26504"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Katerina S.","family":"Karadima","sequence":"additional","affiliation":[{"name":"University of Patras , , ,","place":["Patras, Greece, GR 26504"]},{"name":"Institute of Chemical Engineering Sciences (ICE\u2212HT\/FORTH) , ,","place":["Patras, Greece, GR 26504"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ioanna","family":"Papageorgiou","sequence":"additional","affiliation":[{"name":"University of Patras , , ,","place":["Patras, Greece, GR 26504"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3817-7755","authenticated-orcid":true,"given":"Georgios G.","family":"Vogiatzis","sequence":"additional","affiliation":[{"name":"University of Patras , , ,","place":["Patras, Greece, GR 26504"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3599-0676","authenticated-orcid":true,"given":"Vlasis G.","family":"Mavrantzas","sequence":"additional","affiliation":[{"name":"University of Patras , , ,","place":["Patras, Greece, GR 26504"]},{"name":"Institute of Chemical Engineering Sciences (ICE\u2212HT\/FORTH) , ,","place":["Patras, Greece, GR 26504"]},{"name":"ETH Zu\u0308rich , , ,","place":["Zu\u0308rich, Switzerland, CH-8092"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2026,10,2]]},"reference":[{"issue":"10325","key":"2026101508071575400_cit1","doi-asserted-by":"publisher","first-page":"629","DOI":"10.1016\/S0140-6736(21)02724-0","article-title":"Global Burden of Bacterial\nAntimicrobial Resistance in 2019: A Systematic Analysis","volume":"399","author":"Murray","year":"2022","journal-title":"Lancet"},{"issue":"1","key":"2026101508071575400_cit2","doi-asserted-by":"publisher","first-page":"48","DOI":"10.1186\/s40779-021-00343-2","article-title":"Antimicrobial Peptides: Mechanism\nof Action, Activity and Clinical\nPotential","volume":"8","author":"Zhang","year":"2021","journal-title":"Military Med Res."},{"key":"2026101508071575400_cit3","doi-asserted-by":"publisher","first-page":"11","DOI":"10.3389\/fmicb.2020.582779","article-title":"Antimicrobial Peptides:\nClassification, Design, Application and Research Progress in Multiple\nFields","volume":"11","author":"Huan","year":"2020","journal-title":"Front. Microbiol."},{"issue":"8","key":"2026101508071575400_cit4","doi-asserted-by":"publisher","first-page":"3926","DOI":"10.3390\/ijms22083926","article-title":"Antibacterial\nand\nAntibiofilm Activities of Novel Antimicrobial Peptides against Multidrug-Resistant\nEnterotoxigenic Escherichia Coli","volume":"22","author":"Wu","year":"2021","journal-title":"Int. J. Mol. Sci."},{"issue":"6","key":"2026101508071575400_cit5","doi-asserted-by":"publisher","first-page":"867","DOI":"10.3390\/microorganisms8060867","article-title":"Shorter Antibacterial\nPeptide Having High Selectivity for E. Coli Membranes and Low Potential for Inducing Resistance","volume":"8","author":"Barreto-Santamari\u0301a","year":"2020","journal-title":"Microorganisms"},{"issue":"7","key":"2026101508071575400_cit6","doi-asserted-by":"publisher","first-page":"4113","DOI":"10.1128\/AAC.02578-14","article-title":"Targeting\nMethicillin-Resistant\nStaphylococcus Aureus with Short Salt-Resistant Synthetic Peptides","volume":"58","author":"Mohamed","year":"2014","journal-title":"Antimicrob. Agents Chemother."},{"key":"2026101508071575400_cit7","doi-asserted-by":"publisher","DOI":"10.3389\/fmicb.2022.1029366","article-title":"A Designed Antimicrobial Peptide with Potential\nAbility against Methicillin\nResistant Staphylococcus Aureus","volume":"13","author":"Yuan","year":"2022","journal-title":"Front. Microbiol."},{"issue":"1","key":"2026101508071575400_cit8","doi-asserted-by":"publisher","first-page":"24","DOI":"10.3390\/antibiotics9010024","article-title":"Development and\nChallenges of Antimicrobial Peptides for Therapeutic\nApplications","volume":"9","author":"Chen","year":"2020","journal-title":"Antibiotics"},{"issue":"9","key":"2026101508071575400_cit9","doi-asserted-by":"publisher","first-page":"464","DOI":"10.1016\/j.tibtech.2011.05.001","article-title":"The Expanding\nScope of Antimicrobial\nPeptide Structures and Their Modes of Action","volume":"29","author":"Nguyen","year":"2011","journal-title":"Trends Biotechnol."},{"issue":"22","key":"2026101508071575400_cit10","doi-asserted-by":"publisher","first-page":"6483","DOI":"10.1111\/j.1742-4658.2009.07359.x","article-title":"Multifunctional\nHost Defense Peptides: Intracellular-Targeting Antimicrobial Peptides","volume":"276","author":"Nicolas","year":"2009","journal-title":"FEBS J."},{"issue":"11","key":"2026101508071575400_cit11","doi-asserted-by":"publisher","first-page":"540","DOI":"10.3390\/fermentation10110540","article-title":"A Review of\nAntimicrobial Peptides:\nStructure, Mechanism of Action, and Molecular Optimization Strategies","volume":"10","author":"Ma","year":"2024","journal-title":"Fermentation"},{"issue":"9","key":"2026101508071575400_cit12","doi-asserted-by":"publisher","DOI":"10.1016\/S1473-3099(20)30327-3","article-title":"The\nValue of Antimicrobial\nPeptides in the Age of Resistance","volume":"20","author":"Magana","year":"2020","journal-title":"Lancet Infect.\nDis."},{"key":"2026101508071575400_cit13","doi-asserted-by":"publisher","first-page":"444","DOI":"10.1016\/j.foodcont.2014.07.050","article-title":"The Antimicrobial\nEffects\nand Synergistic Antibacterial Mechanism of the Combination of \u03b5-Polylysine\nand Nisin against Bacillus Subtilis","volume":"47","author":"Liu","year":"2015","journal-title":"Food Control"},{"key":"2026101508071575400_cit14","doi-asserted-by":"publisher","first-page":"10","DOI":"10.3389\/fmicb.2019.02719","article-title":"Synergistic\nAntibacterial Activity of Designed Trp-Containing Antibacterial Peptides\nin Combination With Antibiotics Against Multidrug-Resistant Staphylococcus\nEpidermidis","volume":"10","author":"Shang","year":"2019","journal-title":"Front. Microbiol."},{"key":"2026101508071575400_cit15","doi-asserted-by":"publisher","first-page":"13","DOI":"10.3389\/fmicb.2022.953720","article-title":"Synergistic Antimicrobial Effect\nof Antimicrobial Peptides CATH-1,\nCATH-3, and PMAP-36 With Erythromycin Against Bacterial Pathogens","volume":"13","author":"Lu","year":"2022","journal-title":"Front. Microbiol."},{"issue":"10","key":"2026101508071575400_cit16","doi-asserted-by":"publisher","first-page":"5719","DOI":"10.1128\/AAC.02542-14","article-title":"Synergistic\nEffects of Antimicrobial Peptides and Antibiotics against Clostridium\nDifficile","volume":"58","author":"Nuding","year":"2014","journal-title":"Antimicrob. Agents Chemother."},{"issue":"40","key":"2026101508071575400_cit17","doi-asserted-by":"publisher","first-page":"9756","DOI":"10.1021\/acs.jpcb.4c03766","article-title":"Understanding Antimicrobial Peptide Synergy: Differential\nBinding Interactions and Their Impact on Membrane Integrity","volume":"128","author":"Yoon","year":"2024","journal-title":"J. Phys. Chem. B"},{"issue":"25","key":"2026101508071575400_cit18","doi-asserted-by":"publisher","first-page":"6049","DOI":"10.1021\/acs.jpcb.4c02387","article-title":"Molecular Dynamics Simulations Help\nDetermine the Molecular Mechanisms\nof Lasioglossin-III and Its Variant Peptides\u2019 Membrane Interfacial\nInteractions","volume":"128","author":"Kumar","year":"2024","journal-title":"J. Phys. Chem. B"},{"issue":"5","key":"2026101508071575400_cit19","doi-asserted-by":"publisher","first-page":"1106","DOI":"10.1021\/acs.accounts.7b00613","article-title":"Molecular Dynamics Simulations Are Redefining Our View\nof Peptides Interacting with Biological Membranes","volume":"51","author":"Ulmschneider","year":"2018","journal-title":"Acc. Chem. Res."},{"issue":"3","key":"2026101508071575400_cit20","doi-asserted-by":"publisher","first-page":"369","DOI":"10.1002\/bip.20911","article-title":"Effects of Net Charge\nand the Number of Positively\nCharged Residues on the Biological Activity of Amphipathic \u03b1-Helical\nCationic Antimicrobial Peptides","volume":"90","author":"Jiang","year":"2008","journal-title":"Pept. Sci."},{"issue":"18","key":"2026101508071575400_cit21","doi-asserted-by":"publisher","first-page":"3547","DOI":"10.1016\/j.jmb.2018.12.015","article-title":"Peptide Design\nPrinciples for Antimicrobial Applications","volume":"431","author":"Torres","year":"2019","journal-title":"J.\nMol. Biol."},{"key":"2026101508071575400_cit22","doi-asserted-by":"publisher","first-page":"116224","DOI":"10.1016\/j.ejmech.2024.116224","article-title":"The Antibacterial Properties\nof Branched Peptides Based on Poly(l-Arginine): In Vitro Antibacterial Evaluation and Molecular Dynamic Simulations","volume":"268","author":"Eloi\u0308se","year":"2024","journal-title":"Eur. J. Med. Chem."},{"key":"2026101508071575400_cit23","doi-asserted-by":"publisher","DOI":"10.3389\/fmolb.2024.1429163","article-title":"Branched Oncolytic\nPeptides Target HSPGs, Inhibit Metastasis, and Trigger the Release\nof Molecular Determinants of Immunogenic Cell Death in Pancreatic\nCancer","volume":"11","author":"Rencinai","year":"2024","journal-title":"Front. Mol. Biosci."},{"issue":"14","key":"2026101508071575400_cit24","doi-asserted-by":"publisher","first-page":"3009","DOI":"10.1039\/D4CC06442A","article-title":"Assembling\nBranched and Macrocyclic Peptides on Proteins","volume":"61","author":"Ullrich","year":"2025","journal-title":"Chem. Commun."},{"issue":"14","key":"2026101508071575400_cit25","doi-asserted-by":"publisher","first-page":"6577","DOI":"10.1039\/D1NJ05353A","article-title":"The Antimicrobial Cyclic\nPeptide B2 Combats Multidrug Resistant Acinetobacter\nBaumannii Infection","volume":"46","author":"He","year":"2022","journal-title":"New J. Chem."},{"issue":"5","key":"2026101508071575400_cit26","doi-asserted-by":"publisher","first-page":"1125","DOI":"10.1021\/acschembio.4c00076","article-title":"Computational Design of Cyclic Peptide Inhibitors of a Bacterial\nMembrane Lipoprotein Peptidase","volume":"19","author":"Craven","year":"2024","journal-title":"ACS Chem. Biol."},{"issue":"8","key":"2026101508071575400_cit27","doi-asserted-by":"publisher","first-page":"1687","DOI":"10.1016\/j.bbamem.2008.09.013","article-title":"Control of\nCell Selectivity of Antimicrobial Peptides","volume":"1788","author":"Matsuzaki","year":"2009","journal-title":"Biochim. Biophys. Acta"},{"issue":"1","key":"2026101508071575400_cit28","doi-asserted-by":"publisher","first-page":"4","DOI":"10.3390\/biom8010004","article-title":"Antimicrobial Peptides: Diversity,\nMechanism of Action and Strategies to Improve the Activity and Biocompatibility\nIn Vivo","volume":"8","author":"Kumar","year":"2018","journal-title":"Biomolecules"},{"issue":"9","key":"2026101508071575400_cit29","doi-asserted-by":"publisher","DOI":"10.1016\/j.heliyon.2023.e19641","article-title":"De Novo Peptides\nas Potential Antimicrobial Agents","volume":"9","author":"Amarh","year":"2023","journal-title":"Heliyon"},{"issue":"29","key":"2026101508071575400_cit30","doi-asserted-by":"publisher","first-page":"8347","DOI":"10.1021\/bi000946l","article-title":"Action\nof Antimicrobial Peptides: Two-State Model","volume":"39","author":"Huang","year":"2000","journal-title":"Biochemistry"},{"issue":"3","key":"2026101508071575400_cit31","doi-asserted-by":"publisher","first-page":"469","DOI":"10.1007\/s00232-014-9759-4","article-title":"Implicit Membrane Investigation of the Stability of\nAntimicrobial Peptide \u03b2-Barrels and Arcs","volume":"248","author":"Lipkin","year":"2015","journal-title":"J. Membr. Biol."},{"issue":"52","key":"2026101508071575400_cit32","doi-asserted-by":"publisher","first-page":"21223","DOI":"10.1073\/pnas.1201559110","article-title":"Direct Visualization\nof the Alamethicin\nPore Formed in a Planar Phospholipid Matrix","volume":"109","author":"Pieta","year":"2012","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"1","key":"2026101508071575400_cit33","doi-asserted-by":"publisher","first-page":"13535","DOI":"10.1038\/ncomms13535","article-title":"Spontaneous Formation of Structurally\nDiverse Membrane\nChannel Architectures from a Single Antimicrobial Peptide","volume":"7","author":"Wang","year":"2016","journal-title":"Nat. Commun."},{"issue":"8","key":"2026101508071575400_cit34","doi-asserted-by":"publisher","first-page":"1485","DOI":"10.1016\/j.bbamem.2010.04.004","article-title":"Antimicrobial Peptides in Toroidal and Cylindrical\nPores","volume":"1798","author":"Mihajlovic","year":"2010","journal-title":"Biochim. Biophys. Acta"},{"issue":"26","key":"2026101508071575400_cit35","doi-asserted-by":"publisher","first-page":"7163","DOI":"10.1021\/acs.jpcb.1c01954","article-title":"Molecular\nInsights into Pore Formation Mechanism, Membrane Perturbation, and\nWater Permeation by the Antimicrobial Peptide Pleurocidin: A Combined\nAll-Atom and Coarse-Grained Molecular Dynamics Simulation Study","volume":"125","author":"Talandashti","year":"2021","journal-title":"J. Phys. Chem. B"},{"issue":"6","key":"2026101508071575400_cit36","doi-asserted-by":"publisher","first-page":"665","DOI":"10.1007\/s00232-022-00258-6","article-title":"A Molecular Dynamics\nStudy of Antimicrobial Peptide\nInteractions with the Lipopolysaccharides of the Outer Bacterial Membrane","volume":"255","author":"Sharma","year":"2022","journal-title":"J. Membr. Biol."},{"issue":"20","key":"2026101508071575400_cit37","doi-asserted-by":"publisher","first-page":"4955","DOI":"10.1021\/acs.jcim.2c00437","article-title":"Molecular\nModeling and Simulation of the Peptidoglycan Layer of Gram-Positive\nBacteria Staphylococcus Aureus","volume":"62","author":"Pokhrel","year":"2022","journal-title":"J. Chem. Inf.\nModel."},{"issue":"10","key":"2026101508071575400_cit38","doi-asserted-by":"publisher","first-page":"4070","DOI":"10.3390\/molecules28104070","article-title":"Aggregation of Amyloidogenic Peptide\nUperin-Molecular Dynamics Simulations","volume":"28","author":"Ermakova","year":"2023","journal-title":"Molecules"},{"issue":"7","key":"2026101508071575400_cit39","doi-asserted-by":"publisher","first-page":"1235","DOI":"10.3390\/molecules22071235","article-title":"Molecular Dynamics Simulations of\nthe Host Defense Peptide Temporin L and Its Q3K Derivative: An Atomic\nLevel View from Aggregation in Water to Bilayer Perturbation","volume":"22","author":"Farrotti","year":"2017","journal-title":"Molecules"},{"issue":"21","key":"2026101508071575400_cit40","doi-asserted-by":"publisher","first-page":"5450","DOI":"10.3390\/ijms20215450","article-title":"Self-Association\nof\nAntimicrobial Peptides: A Molecular Dynamics Simulation Study on Bombinin","volume":"20","author":"Petkov","year":"2019","journal-title":"Int. J. Mol. Sci."},{"issue":"19","key":"2026101508071575400_cit41","doi-asserted-by":"publisher","first-page":"4208","DOI":"10.1021\/acs.jpcb.2c08576","article-title":"Self-Assembly of Phenylalanine-Leucine, Leucine-Phenylalanine,\nand Cyclo(-Leucine-Phenylalanine) Dipeptides through Simulations and\nExperiments","volume":"127","author":"Divanach","year":"2023","journal-title":"J. Phys. Chem. B"},{"issue":"9","key":"2026101508071575400_cit42","doi-asserted-by":"publisher","first-page":"2370","DOI":"10.1080\/07391102.2018.1484814","article-title":"Antimicrobial Cell Penetrating Peptides\nwith Bacterial Cell Specificity: Pharmacophore Modelling, Quantitative\nStructure Activity Relationship and Molecular Dynamics Simulation","volume":"37","author":"Faya","year":"2019","journal-title":"J. Biomol. Struct. Dyn."},{"issue":"3","key":"2026101508071575400_cit43","doi-asserted-by":"publisher","first-page":"904","DOI":"10.1021\/acs.molpharmaceut.1c00883","article-title":"Aggregation\nBehavior\nof Structurally Similar Therapeutic Peptides Investigated by 1H NMR\nand All-Atom Molecular Dynamics Simulations","volume":"19","author":"Hjalte","year":"2022","journal-title":"Mol. Pharmaceutics"},{"issue":"21","key":"2026101508071575400_cit44","doi-asserted-by":"publisher","first-page":"9501","DOI":"10.1021\/acs.jpclett.0c02094","article-title":"Aggregation State of Synergistic\nAntimicrobial Peptides","volume":"11","author":"Remington","year":"2020","journal-title":"J. Phys. Chem. Lett."},{"issue":"7","key":"2026101508071575400_cit45","doi-asserted-by":"publisher","first-page":"3208","DOI":"10.1529\/biophysj.108.136226","article-title":"Peptide Aggregation\nin Finite Systems","volume":"95","author":"Singh","year":"2008","journal-title":"Biophys. J."},{"issue":"6","key":"2026101508071575400_cit46","doi-asserted-by":"publisher","first-page":"20170030","DOI":"10.1098\/rsfs.2017.0030","article-title":"Factors Affecting\nthe Physical Stability (Aggregation) of Peptide Therapeutics","volume":"7","author":"Zapadka","year":"2017","journal-title":"Interface Focus"},{"issue":"52","key":"2026101508071575400_cit47","doi-asserted-by":"publisher","DOI":"10.1002\/chem.202400080","article-title":"A Peptide Strategy for Inhibiting Different\nProtein Aggregation Pathways","volume":"30","author":"Garfagnini","year":"2024","journal-title":"Chem. - Eur. J."},{"issue":"1","key":"2026101508071575400_cit48","doi-asserted-by":"publisher","first-page":"269","DOI":"10.1039\/D4NA00614C","article-title":"A Secondary Structure\nwithin Small Peptides Guiding Spontaneous Self-Aggregation and Nanoparticle\nFormation","volume":"7","author":"Marti\u0301nez-Flores","year":"2024","journal-title":"Nanoscale Adv."},{"issue":"1","key":"2026101508071575400_cit49","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0054175","article-title":"A Consensus\nMethod for the Prediction of \u2018Aggregation-Prone\u2019 Peptides\nin Globular Proteins","volume":"8","author":"Tsolis","year":"2013","journal-title":"PLoS One"},{"issue":"9","key":"2026101508071575400_cit50","doi-asserted-by":"publisher","first-page":"3567","DOI":"10.1021\/jacsau.4c00501","article-title":"Aggregation\nRules of Short Peptides","volume":"4","author":"Wang","year":"2024","journal-title":"JACS Au"},{"issue":"2","key":"2026101508071575400_cit51","doi-asserted-by":"publisher","first-page":"021302","DOI":"10.1063\/5.0180691","article-title":"Advanced Computational\nApproaches\nto Understand Protein Aggregation","volume":"5","author":"Ghosh","year":"2024","journal-title":"Biophysics\nRev."},{"issue":"4","key":"2026101508071575400_cit52","doi-asserted-by":"publisher","first-page":"677","DOI":"10.1038\/s41557-026-02090-0","article-title":"Amino Acid\nComposition Drives Aggregation during Peptide Synthesis","volume":"18","author":"Tama\u0301s","year":"2026","journal-title":"Nat. Chem."},{"issue":"9","key":"2026101508071575400_cit53","doi-asserted-by":"publisher","first-page":"2909","DOI":"10.1002\/jps.21566","article-title":"Protein Aggregation:\nPathways, Induction Factors and Analysis","volume":"98","author":"Mahler","year":"2009","journal-title":"J.\nPharm. Sci."},{"issue":"1","key":"2026101508071575400_cit54","doi-asserted-by":"publisher","first-page":"215","DOI":"10.1039\/C9RA09350H","article-title":"Aggregation of Biologically Important Peptides and\nProteins: Inhibition or Acceleration Depending on Protein and Metal\nIon Concentrations","volume":"10","author":"Poulson","year":"2020","journal-title":"RSC Adv."},{"issue":"20","key":"2026101508071575400_cit55","doi-asserted-by":"publisher","first-page":"4854","DOI":"10.3390\/molecules25204854","article-title":"Evaluation\nof Peptide\/Protein Self-Assembly\nand Aggregation by Spectroscopic Methods","volume":"25","author":"Pignataro","year":"2020","journal-title":"Molecules"},{"issue":"1","key":"2026101508071575400_cit56","doi-asserted-by":"publisher","first-page":"13206","DOI":"10.1038\/s41598-020-69995-9","article-title":"Correlation\nbetween Hemolytic Activity, Cytotoxicity and Systemic in Vivo Toxicity\nof Synthetic Antimicrobial Peptides","volume":"10","author":"Greco","year":"2020","journal-title":"Sci. Rep."},{"key":"2026101508071575400_cit57","doi-asserted-by":"publisher","first-page":"257","DOI":"10.1007\/978-3-319-97277-0_21","article-title":"Molecular Dynamics Study of\nthe Solution Behaviour of Antimicrobial Peptide Indolicidin","volume-title":"Advanced Computing in Industrial Mathematics: 12th Annual\nMeeting of the Bulgarian Section of SIAM Sofia, Bulgaria Revised Selected\nPapers","author":"Marinova","year":"2019"},{"key":"2026101508071575400_cit58","doi-asserted-by":"publisher","DOI":"10.1002\/advs.202105868","article-title":"Peptide Aggregation Induced Immunogenic Rupture (PAIIR)","volume":"9","author":"Gunay","year":"2022","journal-title":"Adv. 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