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Despite extensive research, no effective therapeutics are yet available to treat these chronic degenerative diseases. Targeting the aggregation of disease-specific proteins is regarded as a promising new approach to treat these diseases. In the past few years, rapid progress in this field has been made in vitro, in vivo, and in silico to generate potential drug candidates, ranging from small molecules to polymers to nanoparticles. Small molecular probes, mostly those derived from natural sources, have been of particular interest among amyloid inhibitors. Here, we summarize some of the most important natural small molecular probes which can inhibit the aggregation of A\u03b2, hIAPP, and \u03b1-syn peptides and discuss how their binding efficacy and preference for the peptides vary with their structure and conformation. This provides a comprehensive idea of the crucial factors which should be incorporated into the future design of novel drug candidates useful for the treatment of amyloid diseases.<\/jats:p>","DOI":"10.1021\/acs.jpcb.2c07607","type":"journal-article","created":{"date-parts":[[2023,1,13]],"date-time":"2023-01-13T19:11:21Z","timestamp":1673637081000},"page":"600-615","source":"Crossref","is-referenced-by-count":30,"title":["Illustrating the\nEffect of Small Molecules Derived\nfrom Natural Resources on Amyloid Peptides"],"prefix":"10.1021","volume":"127","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-7771-5325","authenticated-orcid":true,"given":"Rituparna","family":"Roy","sequence":"first","affiliation":[{"name":"Indian Institute of Technology , , - ,","place":["Guwahati\nAssam, India, 781039"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9693-2915","authenticated-orcid":true,"given":"Sandip","family":"Paul","sequence":"additional","affiliation":[{"name":"Indian Institute of Technology , , - ,","place":["Guwahati\nAssam, India, 781039"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2023,1,13]]},"reference":[{"key":"2026081804431704300_cit1","doi-asserted-by":"publisher","first-page":"2545","DOI":"10.1021\/acs.chemrev.0c01122","article-title":"Amyloid Oligomers: A Joint Experimental\/Computational\nPerspective on Alzheimer\u2019s Disease, Parkinson\u2019s Disease,\nType II Diabetes, and Amyotrophic Lateral Sclerosis","volume":"121","author":"Nguyen","year":"2021","journal-title":"Chem. 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Bio."},{"key":"2026081804431704300_cit5","doi-asserted-by":"publisher","first-page":"1519","DOI":"10.3390\/molecules24081519","article-title":"Natural Products\nin Alzheimer\u2019s Disease Therapy: Would Old Therapeutic Approaches\nFix the Broken Promise of Modern Medicines?","volume":"24","author":"Habtemariam","year":"2019","journal-title":"Molecules"},{"key":"2026081804431704300_cit6","doi-asserted-by":"publisher","first-page":"13434","DOI":"10.1039\/C5CC05264E","article-title":"Function and Toxicity of Amyloid\nBeta and Recent Therapeutic Interventions Targeting Amyloid Beta in\nAlzheimer\u2019s Disease","volume":"51","author":"Rajasekhar","year":"2015","journal-title":"Chem. Commun."},{"key":"2026081804431704300_cit7","doi-asserted-by":"publisher","first-page":"10823","DOI":"10.1021\/jm301182j","article-title":"Small Molecules\nThat Target Protein\nMisfolding","volume":"55","author":"Gavrin","year":"2012","journal-title":"J. Med. Chem."},{"key":"2026081804431704300_cit8","doi-asserted-by":"publisher","first-page":"1300","DOI":"10.1021\/acschemneuro.6b00175","article-title":"Natural Tripeptide-Based\nInhibitor\nof Multifaceted Amyloid \u03b2 Toxicity","volume":"7","author":"Rajasekhar","year":"2016","journal-title":"ACS\nChem. Neurosci."},{"key":"2026081804431704300_cit9","doi-asserted-by":"publisher","first-page":"5451","DOI":"10.1038\/s41467-022-32951-4","article-title":"Structure-Based Discovery of Small Molecules\nthat Disaggregate Alzheimer\u2019s Disease Tissue Derived Tau Fibrils\nin vitro","volume":"13","author":"Seidler","year":"2022","journal-title":"Nat. Commun."},{"key":"2026081804431704300_cit10","doi-asserted-by":"publisher","first-page":"3611","DOI":"10.1021\/acschemneuro.9b00216","article-title":"Small Molecule\nInhibits Metal-Dependent and -Independent Multifaceted Toxicity of\nAlzheimer\u2019s Disease","volume":"10","author":"Samanta","year":"2019","journal-title":"ACS Chem. Neurosci."},{"key":"2026081804431704300_cit11","doi-asserted-by":"publisher","first-page":"1309","DOI":"10.3390\/cells10061309","article-title":"Neuroprotective Natural\nProducts for Alzheimer\u2019s Disease","volume":"10","author":"Chen","year":"2021","journal-title":"Cells"},{"key":"2026081804431704300_cit12","doi-asserted-by":"publisher","first-page":"40","DOI":"10.1016\/j.bcp.2017.04.004","article-title":"Natural Product-Based\nAmyloid Inhibitors","volume":"139","author":"Velander","year":"2017","journal-title":"Biochem. Pharmacol."},{"key":"2026081804431704300_cit13","doi-asserted-by":"publisher","DOI":"10.1126\/sciadv.abb5924","article-title":"Small-Molecule Sequestration\nof Amyloid-\u03b2 as a Drug Discovery Strategy for Alzheimer\u2019s\nDisease","volume":"6","author":"Heller","year":"2020","journal-title":"Sci. Adv."},{"key":"2026081804431704300_cit14","doi-asserted-by":"publisher","first-page":"1737","DOI":"10.1021\/acschemneuro.1c00104","article-title":"From Small Molecules\nto Synthesized Polymers: Potential Role in Combating Amyloidogenic\nDisorders","volume":"12","author":"Ghosh","year":"2021","journal-title":"ACS Chem. Neurosci."},{"key":"2026081804431704300_cit15","doi-asserted-by":"publisher","first-page":"3521","DOI":"10.1007\/s00018-018-2872-2","article-title":"Inhibition\nof Protein Misfolding and Aggregation by\nNatural Phenolic Compounds","volume":"75","author":"Dhouafli","year":"2018","journal-title":"Cell. Mol. Life\nSci."},{"key":"2026081804431704300_cit16","doi-asserted-by":"publisher","first-page":"2915","DOI":"10.1021\/acschemneuro.0c00381","article-title":"Potential Role of Natural\nPolyphenols against Protein Aggregation Toxicity: In Vitro, In Vivo,\nand Clinical Studies","volume":"11","author":"Henri\u0301quez","year":"2020","journal-title":"ACS Chem. Neurosci."},{"key":"2026081804431704300_cit17","doi-asserted-by":"publisher","first-page":"295","DOI":"10.1016\/j.jmgm.2017.09.004","article-title":"Combined In\nSilico Approaches for the Identification of Novel Inhibitors of Human\nIslet Amyloid Polypeptide (hIAPP) Fibrillation","volume":"77","author":"Patel","year":"2017","journal-title":"J. Mol. Graph. Model."},{"key":"2026081804431704300_cit18","doi-asserted-by":"publisher","first-page":"11879","DOI":"10.1021\/jp202640b","article-title":"Molecular Insight into Conformational Transition of\nAmyloid \u03b2-Peptide 42 Inhibited by (\u2212)-Epigallocatechin-3-gallate\nProbed by Molecular Simulations","volume":"115","author":"Liu","year":"2011","journal-title":"J. Phys. Chem.\nB"},{"key":"2026081804431704300_cit19","doi-asserted-by":"publisher","first-page":"8286","DOI":"10.1021\/acsabm.0c01234","article-title":"Introduction\nand Fundamentals\nof Human Islet Amyloid Polypeptide Inhibitors","volume":"3","author":"Tang","year":"2020","journal-title":"ACS Appl. Bio Mater."},{"key":"2026081804431704300_cit20","doi-asserted-by":"publisher","first-page":"4351","DOI":"10.1021\/acschemneuro.0c00598","article-title":"Epigallocatechin Gallate Destabilizes\n\u03b1-Synuclein Fibril by Disrupting the E46\u2013K80 Salt-Bridge\nand Inter-protofibril Interface","volume":"11","author":"Yao","year":"2020","journal-title":"ACS Chem. Neurosci."},{"key":"2026081804431704300_cit21","doi-asserted-by":"publisher","first-page":"33076","DOI":"10.1038\/srep33076","article-title":"Conformational Ensemble\nof hIAPP Dimer: Insight into the Molecular Mechanism by which a Green\nTea Extract Inhibits hIAPP Aggregation","volume":"6","author":"Mo","year":"2016","journal-title":"Sci.\nRep."},{"key":"2026081804431704300_cit22","doi-asserted-by":"publisher","first-page":"e94796","DOI":"10.1371\/journal.pone.0094796","article-title":"Exploring the Influence\nof EGCG on the \u03b2-Sheet-Rich Oligomers of Human Islet Amyloid\nPolypeptide (hIAPP1\u201337) and Identifying Its Possible Binding\nSites from Molecular Dynamics Simulation","volume":"9","author":"Wang","year":"2014","journal-title":"PLoS\nOne"},{"key":"2026081804431704300_cit23","doi-asserted-by":"publisher","first-page":"1611","DOI":"10.1002\/cphc.201700057","article-title":"Inhibitory Mechanism\nof Epigallocatechin Gallate on Fibrillation\nand Aggregation of Amidated Human Islet Amyloid Polypeptide","volume":"18","author":"Xu","year":"2017","journal-title":"ChemPhysChem"},{"key":"2026081804431704300_cit24","doi-asserted-by":"publisher","first-page":"105024","DOI":"10.1016\/j.chemphyslip.2020.105024","article-title":"Green Tea Extract EGCG\nplays a Dual Role in A\u03b242 Protofibril Disruption and Membrane\nProtection: A Molecular Dynamic Study","volume":"234","author":"Dong","year":"2021","journal-title":"Chem.\nPhys. 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Neurosci."},{"key":"2026081804431704300_cit27","doi-asserted-by":"publisher","first-page":"492","DOI":"10.1016\/j.jff.2018.11.018","article-title":"A-type\nEGCG Dimer, a New Proanthocyanidins\nDimer from Persimmon Fruits, Interacts with the Amino Acid Residues\nof A\u03b240 which Possessed High Aggregation-Propensity and Strongly\nInhibits its Amyloid Fibrils Formation","volume":"52","author":"Nie","year":"2019","journal-title":"J. Funct.\nFoods"},{"key":"2026081804431704300_cit28","doi-asserted-by":"publisher","first-page":"1399","DOI":"10.1021\/acs.jcim.9b01074","article-title":"Impact\nof the Astaxanthin, Betanin, and EGCG Compounds on Small Oligomers\nof Amyloid A\u03b240 Peptide","volume":"60","author":"Minh\nHung","year":"2020","journal-title":"J. Chem. Inf.\nModel."},{"key":"2026081804431704300_cit29","doi-asserted-by":"publisher","first-page":"1116","DOI":"10.1038\/s41598-017-18807-8","article-title":"Epigallocatechin Gallate\n(EGCG) Reduces the Intensity of Pancreatic Amyloid Fibrils in Human\nIslet Amyloid Polypeptide (hIAPP) Transgenic Mice","volume":"8","author":"Franko","year":"2018","journal-title":"Sci. Rep."},{"key":"2026081804431704300_cit30","doi-asserted-by":"publisher","first-page":"4135","DOI":"10.1021\/jm3017317","article-title":"Progress and Developments in Tau\nAggregation Inhibitors for Alzheimer Disease","volume":"56","author":"Bulic","year":"2013","journal-title":"J. Med. Chem."},{"key":"2026081804431704300_cit31","doi-asserted-by":"publisher","first-page":"6336","DOI":"10.1016\/j.bmcl.2013.09.071","article-title":"Gallic Acid is the Major Component of Grape Seed Extract\nthat Inhibits Amyloid Fibril Formation","volume":"23","author":"Liu","year":"2013","journal-title":"Bioorg.\nMed. Chem. Lett."},{"key":"2026081804431704300_cit32","doi-asserted-by":"publisher","first-page":"67","DOI":"10.1016\/j.nbd.2018.11.009","article-title":"Gallic Acid Disruption of A\u03b21\u201342 Aggregation\nRescues Cognitive Decline of APP\/PS1 Double Transgenic Mouse","volume":"124","author":"Yu","year":"2019","journal-title":"Neurobiol. Dis."},{"key":"2026081804431704300_cit33","doi-asserted-by":"publisher","first-page":"197","DOI":"10.3389\/fnagi.2014.00197","article-title":"Structure Activity\nRelationship of Phenolic Acid Inhibitors of \u03b1-synuclein Fibril\nFormation and Toxicity","volume":"6","author":"Ardah","year":"2014","journal-title":"Front. Aging Neurosci."},{"key":"2026081804431704300_cit34","doi-asserted-by":"publisher","first-page":"34","DOI":"10.3109\/13506129.2012.762761","article-title":"IAPP Aggregation\nand Cellular Toxicity are Inhibited by 1,2,3,4,6-penta-O-galloyl-\u03b2-d-glucose","volume":"20","author":"Bruno","year":"2013","journal-title":"Amyloid"},{"key":"2026081804431704300_cit35","doi-asserted-by":"publisher","first-page":"8155","DOI":"10.1021\/acs.jpcb.2c04230","article-title":"Insights into Molecular Mechanisms\nof EGCG and Apigenin on Disrupting\nAmyloid-Beta Protofibrils Based on Molecular Dynamics Simulations","volume":"126","author":"Fang","year":"2022","journal-title":"J. Phys. Chem. B"},{"key":"2026081804431704300_cit36","doi-asserted-by":"publisher","first-page":"1113","DOI":"10.1016\/j.febslet.2011.03.046","article-title":"Inhibition and Disaggregation of\n\u03b1-synuclein\nOligomers by Natural Polyphenolic Compounds","volume":"585","author":"Caruana","year":"2011","journal-title":"FEBS Lett."},{"key":"2026081804431704300_cit37","doi-asserted-by":"publisher","first-page":"435","DOI":"10.1016\/j.ijbiomac.2020.10.202","article-title":"Resistance\nof Nepetin and its Analogs on the Fibril Formation of Human Islet\nAmyloid Polypeptide","volume":"166","author":"Xu","year":"2021","journal-title":"Int. J. Biol. Macromol."},{"key":"2026081804431704300_cit38","doi-asserted-by":"publisher","first-page":"4650","DOI":"10.1039\/D2TB00230B","article-title":"Biflavones\nInhibit the Fibrillation and Cytotoxicity of the Human Islet Amyloid\nPolypeptide","volume":"10","author":"Xu","year":"2022","journal-title":"J. Mater. Chem. B"},{"key":"2026081804431704300_cit39","doi-asserted-by":"publisher","first-page":"1399","DOI":"10.1080\/07391102.2014.951689","article-title":"Atomistic Mechanism\nof Polyphenol Amyloid Aggregation\nInhibitors: Molecular Dynamics Study of Curcumin, Exifone, and Myricetin\nInteraction with the Segment of Tau Peptide Oligomer","volume":"33","author":"Berhanu","year":"2015","journal-title":"J. Biomol. Struct. Dyn."},{"key":"2026081804431704300_cit40","doi-asserted-by":"publisher","first-page":"29103","DOI":"10.1039\/C5CP03991F","article-title":"Computational Insights into the Inhibition and Destabilization\nof\nMorin on the Oligomer of Full-length Human Islet Amyloid Polypeptide","volume":"17","author":"Wang","year":"2015","journal-title":"Phys. Chem. Chem. Phys."},{"key":"2026081804431704300_cit41","doi-asserted-by":"publisher","first-page":"625","DOI":"10.1016\/j.bbrc.2016.11.083","article-title":"Rutin Suppresses Human-Amylin\/hIAPP Misfolding and\nOligomer Formation in-vitro, and Ameliorates Diabetes and its Impacts\nin Human-Amylin\/hIAPP Transgenic Mice","volume":"482","author":"Aitken","year":"2017","journal-title":"Biochem.\nBiophys. Res. Commun."},{"key":"2026081804431704300_cit42","doi-asserted-by":"publisher","first-page":"73","DOI":"10.1186\/s12906-020-2849-1","article-title":"Inhibition of Alpha-Synuclein Seeded Fibril\nFormation and Toxicity by Herbal Medicinal Extracts","volume":"20","author":"Ardah","year":"2020","journal-title":"BMC Complement. Altern. Med."},{"key":"2026081804431704300_cit43","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1177\/1934578X20924859","article-title":"Quantitative\nAnalysis of 7 Compounds in Diospyros Lotus Leaf Extract and Its Biological\nEffects on Neuroprotection and Antineuroinflammation","volume":"15","author":"Kim","year":"2020","journal-title":"Nat. Prod. Commun."},{"key":"2026081804431704300_cit44","doi-asserted-by":"publisher","first-page":"179","DOI":"10.1515\/hsz-2020-0176","article-title":"Myricetin Protects Pancreatic \u03b2-cells\nfrom Human Islet Amyloid Polypeptide (hIAPP) Induced Cytotoxicity\nand Restores Islet Function","volume":"402","author":"Dubey","year":"2021","journal-title":"Biol. Chem."},{"key":"2026081804431704300_cit45","doi-asserted-by":"publisher","first-page":"1215","DOI":"10.1021\/acschemneuro.8b00039","article-title":"Genistein:\nA Dual Inhibitor of Both Amyloid \u03b2\nand Human Islet Amylin Peptides","volume":"9","author":"Ren","year":"2018","journal-title":"ACS Chem. Neurosci."},{"key":"2026081804431704300_cit46","doi-asserted-by":"publisher","first-page":"495","DOI":"10.1016\/j.bbrc.2012.02.042","article-title":"Silibinin\nInhibits the Toxic Aggregation of Human Islet Amyloid Polypeptide","volume":"419","author":"Cheng","year":"2012","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"2026081804431704300_cit47","doi-asserted-by":"publisher","first-page":"140772","DOI":"10.1016\/j.bbapap.2022.140772","article-title":"Silybins Inhibit\nHuman IAPP Amyloid Growth and Toxicity through Stereospecific Interactions","volume":"1870","author":"Garci\u0301a-Vin\u0303uales","year":"2022","journal-title":"Biochim. Biophys. Acta - Proteins Proteom."},{"key":"2026081804431704300_cit48","doi-asserted-by":"publisher","first-page":"1538","DOI":"10.1080\/08927022.2019.1660778","article-title":"Molecular\nMechanics and Quantum Chemical Calculations Unveil the Combating Eeffect\nof Baicalein on Human Islet Amyloid Polypeptide Aggregates","volume":"45","author":"Srinivasan","year":"2019","journal-title":"Mol. Simul."},{"key":"2026081804431704300_cit49","doi-asserted-by":"publisher","first-page":"316","DOI":"10.1016\/j.ijbiomac.2022.08.088","article-title":"Baicalein\nExhibits Differential Effects and Mechanisms towards Disruption of\n\u03b1-Synuclein Fibrils with Different Polymorphs","volume":"220","author":"Yao","year":"2022","journal-title":"Int. J. Biol. Macromol."},{"key":"2026081804431704300_cit50","doi-asserted-by":"publisher","first-page":"16","DOI":"10.1186\/s12964-021-00704-3","article-title":"Baicalein\nInhibits Heparin-induced\nTau Aggregation by Initializing Non-toxic Tau Oligomer Formation","volume":"19","author":"Sonawane","year":"2021","journal-title":"Cell Commun. Signal."},{"key":"2026081804431704300_cit51","doi-asserted-by":"publisher","DOI":"10.1002\/chem.202104240","article-title":"Combined in Silico and in Vitro Approaches\nTo Uncover the Oxidation and Schiff Base Reaction of Baicalein as\nan Inhibitor of Amyloid Protein Aggregation","volume":"28","author":"Bra\u0301s","year":"2022","journal-title":"Chem. - Eur. J."},{"key":"2026081804431704300_cit52","doi-asserted-by":"publisher","first-page":"579","DOI":"10.1007\/s11418-020-01398-6","article-title":"Inhibitory Activities of Phenylpropanoids\nfrom Lycopus Lucidus on Amyloid Aggregation Related to Alzheimer\u2019s\nDisease and Type 2 Diabetes","volume":"74","author":"Sun","year":"2020","journal-title":"J. Nat. Med."},{"key":"2026081804431704300_cit53","doi-asserted-by":"publisher","first-page":"7775","DOI":"10.1021\/acs.langmuir.2c00827","article-title":"Phenylpropanoids\non the Inhibition\nof \u03b2-Amyloid Aggregation and the Movement of These Molecules\nthrough the POPC Lipid Bilayer","volume":"38","author":"Pal","year":"2022","journal-title":"Langmuir"},{"key":"2026081804431704300_cit54","doi-asserted-by":"publisher","first-page":"393","DOI":"10.1021\/cn3001203","article-title":"Curcumin Modulates\n\u03b1-Synuclein Aggregation and\nToxicity","volume":"4","author":"Singh","year":"2013","journal-title":"ACS Chem. Neurosci."},{"key":"2026081804431704300_cit55","doi-asserted-by":"publisher","first-page":"3507","DOI":"10.1007\/s00253-020-10461-x","article-title":"Bidirectional\nInteractions between Curcumin and Gut Microbiota in Transgenic Mice\nwith Alzheimer\u2019s Disease","volume":"104","author":"Sun","year":"2020","journal-title":"Appl. Microbiol.\nBiotechnol."},{"key":"2026081804431704300_cit56","doi-asserted-by":"publisher","first-page":"183251","DOI":"10.1016\/j.bbamem.2020.183251","article-title":"\u03b1-Synuclein\nFibrillation Products Trigger the Release of Hexokinase I from Mitochondria:\nProtection by Curcumin, and Possible Role in Pathogenesis of Parkinson\u2019s\nDisease","volume":"1862","author":"Dehghani","year":"2020","journal-title":"Biochim. Biophys. Acta. 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