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The misfolding of human islet amyloid polypeptide (hIAPP) into toxic oligomers is a pathogenic feature of this disease, due to which the prevention of hIAPP aggregation is considered the rational approach to combat T2D. Hence, we study the role of a catecholamine, norepinephrine, on the amyloid aggregation of hIAPP, which has previously displayed inhibitory effect on amyloid-\u03b2 aggregation. Via all-atom molecular dynamics simulations, we observe that norepinephrine can not only inhibit the aggregation of hIAPP but also partially disassemble the preformed fibrils. For comparison, the influence of two other molecules (aspirin and benzimidazole, both of which have previously reported to have no inhibitory impact on hIAPP aggregation) is also analyzed. We observe that the conformational preference of hIAPP changes from a \u03b2-sheet conformation to a disordered state when norepinephrine is added to the peptides. However, no such effect is observed in the presence of aspirin or benzimidazole. In-depth investigation reveals that the \u03b2-sheets formed between Leu12\u2013His18 and Leu27\u2013Gly33 enhance the peptide\u2013peptide interactions that are broken by norepinephrine, which itself interacts with the peptides via hydrogen bonding, hydrophobic, and aromatic stacking interactions, preferentially with the C-terminal residues of hIAPP. The molecular mechanism action of norepinephrine on hIAPP aggregation can provide useful insight for the drug design against T2D.<\/jats:p>","DOI":"10.1021\/acs.jpcb.0c07830","type":"journal-article","created":{"date-parts":[[2020,11,18]],"date-time":"2020-11-18T22:03:38Z","timestamp":1605737018000},"page":"10913-10929","source":"Crossref","is-referenced-by-count":29,"title":["Theoretical Investigation of the Inhibitory Mechanism\nof Norepinephrine on hIAPP Amyloid Aggregation and the Destabilization\nof Protofibrils"],"prefix":"10.1021","volume":"124","author":[{"given":"Rituparna","family":"Roy","sequence":"first","affiliation":[{"name":"Indian Institute of Technology , , , ,","place":["Guwahati, Assam, 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, Assam, India, 781039"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2020,11,18]]},"reference":[{"key":"2026081805251684000_cit1","doi-asserted-by":"publisher","first-page":"826706","DOI":"10.1155\/2013\/826706","article-title":"Amylin Uncovered: A\nReview on the Polypeptide Responsible\nfor Type II Diabetes","volume":"2013","author":"Pillay","year":"2013","journal-title":"BioMed Res. 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Biophys."},{"key":"2026081805251684000_cit5","doi-asserted-by":"publisher","first-page":"1089","DOI":"10.1021\/bi301525e","article-title":"Comparative Molecular\nDynamics Study of Human Islet Amyloid Polypeptide (IAPP) and Rat IAPP\nOligomers","volume":"52","author":"Liang","year":"2013","journal-title":"Biochemistry"},{"key":"2026081805251684000_cit6","doi-asserted-by":"publisher","first-page":"3132","DOI":"10.1529\/biophysj.107.110635","article-title":"Mechanism of Islet\nAmyloid Polypeptide Fibrillation\nat Lipid Interfaces Studied by Infrared Reflection Absorption Spectroscopy","volume":"93","author":"Lopes","year":"2007","journal-title":"Biophys. 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Mass Spectrom."},{"key":"2026081805251684000_cit11","doi-asserted-by":"publisher","first-page":"396","DOI":"10.1016\/j.cplett.2008.07.110","article-title":"The Role of\nthe Cys2-Cys7 Disulfide Bridge in the Early Steps of Islet Amyloid\nPolypeptide Aggregation: A Molecular Dynamics Study","volume":"463","author":"Milardi","year":"2008","journal-title":"Chem. Phys. 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Dyn."},{"key":"2026081805251684000_cit29","doi-asserted-by":"publisher","first-page":"2235","DOI":"10.2337\/diabetes.54.7.2235","article-title":"Long-Term\nTreatment with Rosiglitazone and Metformin Reduces the Extent of,\nbut Does Not Prevent, Islet Amyloid Deposition in Mice Expressing\nthe Gene for Human Islet Amyloid Polypeptide","volume":"54","author":"Hull","year":"2005","journal-title":"Diabetes"},{"key":"2026081805251684000_cit30","doi-asserted-by":"publisher","first-page":"2046327","DOI":"10.1155\/2016\/2046327","article-title":"Inhibition\nof IAPP Aggregation and Toxicity by Natural Products and Derivatives","volume":"2016","author":"Pithadia","year":"2016","journal-title":"J. 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Acta, Biomembr."},{"key":"2026081805251684000_cit45","doi-asserted-by":"publisher","first-page":"40095","DOI":"10.1038\/srep40095","article-title":"Disaggregation\nof Amylin Aggregate by Novel Conformationally Restricted Aminobenzoic\nAcid containing \u03b1\/\u03b2 and \u03b1\/\u03b3 Hybrid Peptidomimetics","volume":"7","author":"Paul","year":"2017","journal-title":"Sci. Rep."},{"key":"2026081805251684000_cit46","doi-asserted-by":"publisher","first-page":"4041","DOI":"10.1002\/anie.200353565","article-title":"Inhibition of Amyloid\nFibril Formation by Peptide Analogues Modified\nwith \u03b1-Aminoisobutyric Acid","volume":"43","author":"Gilead","year":"2004","journal-title":"Angew. Chem.,\nInt. Ed."},{"key":"2026081805251684000_cit47","doi-asserted-by":"publisher","first-page":"1227","DOI":"10.1016\/j.bpj.2013.07.029","article-title":"Effect of Proline Mutations on the\nMonomer Conformations of Amylin","volume":"105","author":"Chiu","year":"2013","journal-title":"Biophys. 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Biol."},{"key":"2026081805251684000_cit49","doi-asserted-by":"publisher","first-page":"2575","DOI":"10.1002\/1873-3468.12261","article-title":"Peptide Inhibitors of the Amyloidogenesis\nof IAPP: Verification of the Hairpin-Binding Geometry Hypothesis","volume":"590","author":"Sivanesam","year":"2016","journal-title":"FEBS Lett."},{"key":"2026081805251684000_cit50","doi-asserted-by":"publisher","first-page":"8202","DOI":"10.1021\/bi200760h","article-title":"Designed Hairpin Peptides Interfere\nwith Amyloidogenesis Pathways: Fibril Formation and Cytotoxicity Inhibition,\nInterception of the Preamyloid State","volume":"50","author":"Huggins","year":"2011","journal-title":"Biochemistry"},{"key":"2026081805251684000_cit51","doi-asserted-by":"publisher","first-page":"13095","DOI":"10.1002\/anie.201504973","article-title":"A Hot-Segment-Based\nApproach for the Design of Cross-Amyloid Interaction Surface Mimics\nas Inhibitors of Amyloid Self-Assembly","volume":"54","author":"Andreetto","year":"2015","journal-title":"Angew.\nChem., Int. 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