{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,17]],"date-time":"2026-10-17T04:40:38Z","timestamp":1792212038292,"version":"4.4.0"},"reference-count":39,"publisher":"Wiley","issue":"12","license":[{"start":{"date-parts":[[2026,10,16]],"date-time":"2026-10-16T00:00:00Z","timestamp":1792108800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"},{"start":{"date-parts":[[2026,10,16]],"date-time":"2026-10-16T00:00:00Z","timestamp":1792108800000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["1R15DK112172\u201002"],"award-info":[{"award-number":["1R15DK112172\u201002"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Journal of Peptide Science"],"published-print":{"date-parts":[[2026,12]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    Human islet amyloid polypeptide (hIAPP), a 37\u2010residue hormone co\u2010secreted with insulin from pancreatic \u03b2\u2010cells, undergoes self\u2010assembly into cytotoxic amyloid fibrils in the pathogenesis of type 2 diabetes (T2D). The resulting islet amyloid deposits are implicated in progressive \u03b2\u2010cell dysfunction and loss, making hIAPP aggregation an attractive therapeutic target. Nonhuman islet amyloid polypeptide (IAPP) orthologs have recently emerged as a valuable source of mechanistic insight, with several variants\u2014including raccoon and chicken IAPPs\u2014demonstrating the capacity to inhibit hIAPP fibril formation. Here, the biophysical characterization of red panda (\n                    <jats:styled-content style=\"fixed-case\">\n                      <jats:italic>Ailurus fulgens<\/jats:italic>\n                    <\/jats:styled-content>\n                    ) IAPP (rpIAPP) and its effects on hIAPP aggregation are reported. Using thioflavin T fluorescence assays, circular dichroism spectroscopy, and atomic force microscopy, red panda IAPP is found to inhibit hIAPP fibrillation at substoichiometric concentrations, with significant inhibitory activity observed at molar ratios as low as 1:0.5 (hIAPP:rpIAPP). These results position red panda IAPP as one of the more potent nonhuman IAPP inhibitors characterized to date and support its further evaluation as a scaffold for the rational design of peptide\u2010based therapeutics targeting T2D\u2010associated amyloidogenesis.\n                  <\/jats:p>","DOI":"10.1002\/psc.70140","type":"journal-article","created":{"date-parts":[[2026,10,17]],"date-time":"2026-10-17T03:48:19Z","timestamp":1792208899000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Inhibitory Activity of Red Panda Islet Amyloid Polypeptide on Human IAPP Aggregation"],"prefix":"10.1002","volume":"32","author":[{"ORCID":"https:\/\/orcid.org\/0009-0005-4143-0415","authenticated-orcid":false,"given":"Lauren","family":"Phillips","sequence":"first","affiliation":[{"name":"Department of Chemistry and Biochemistry Loyola Marymount University  Los Angeles California USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Elizabeth L.","family":"Moffet","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Biochemistry Loyola Marymount University  Los Angeles California USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Judah","family":"Mayfield","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Biochemistry Loyola Marymount University  Los Angeles California USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Eden L.","family":"Jonick","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Biochemistry Loyola Marymount University  Los Angeles California USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Luiza A.","family":"Nogaj","sequence":"additional","affiliation":[{"name":"Department of Biology Mount Saint Mary's University  Los Angeles California USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7430-861X","authenticated-orcid":false,"given":"David A.","family":"Moffet","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Biochemistry Loyola Marymount University  Los Angeles California USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2026,10,16]]},"reference":[{"key":"e_1_2_10_2_1","unstructured":"Prevention C. f. D. C. a \u201cNational Diabetes Statistics Report \u201d2026 https:\/\/gis.cdc.gov\/grasp\/diabetes\/diabetesatlas\u2010statsreport.html."},{"issue":"3","key":"e_1_2_10_3_1","doi-asserted-by":"crossref","first-page":"795","DOI":"10.1152\/physrev.00042.2009","article-title":"Islet Amyloid Polypeptide, Islet Amyloid, and Diabetes Mellitus","volume":"91","author":"Westermark P.","year":"2011","journal-title":"Physiological Reviews"},{"issue":"8","key":"e_1_2_10_4_1","doi-asserted-by":"crossref","first-page":"3629","DOI":"10.1210\/jc.2004-0405","article-title":"Islet Amyloid: A Critical Entity in the Pathogenesis of Type 2 Diabetes","volume":"89","author":"Hull R. L.","year":"2004","journal-title":"Journal of Clinical Endocrinology and Metabolism"},{"key":"e_1_2_10_5_1","doi-asserted-by":"publisher","DOI":"10.1515\/med\u20102024\u20101124"},{"key":"e_1_2_10_6_1","doi-asserted-by":"publisher","DOI":"10.1021\/acsabm.0c01234"},{"key":"e_1_2_10_7_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.2528103123"},{"key":"e_1_2_10_8_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.93.14.7283"},{"key":"e_1_2_10_9_1","doi-asserted-by":"publisher","DOI":"10.2174\/0929866528666210806152706"},{"issue":"3","key":"e_1_2_10_10_1","doi-asserted-by":"crossref","first-page":"194","DOI":"10.3109\/13506129.2015.1070824","article-title":"Wildlife Sequences of Islet Amyloid Polypeptide (IAPP) Identify Critical Species Variants for Fibrillization","volume":"22","author":"Fortin J. S.","year":"2015","journal-title":"Amyloid: The International Journal of Experimental and Clinical Investigation: The Official Journal of the International Society of Amyloidosis"},{"key":"e_1_2_10_11_1","doi-asserted-by":"publisher","DOI":"10.1002\/psc.3199"},{"key":"e_1_2_10_12_1","doi-asserted-by":"publisher","DOI":"10.1021\/jasms.3c00005"},{"issue":"1","key":"e_1_2_10_13_1","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1016\/j.hermed.2015.11.001","article-title":"Identification of Plant Extracts That Inhibit the Formation of Diabetes\u2010Linked IAPP Amyloid","volume":"6","author":"Fuentes A.","year":"2016","journal-title":"Jornal of Herbal Medicine"},{"key":"e_1_2_10_14_1","doi-asserted-by":"crossref","first-page":"450","DOI":"10.1016\/j.jff.2014.12.013","article-title":"Inhibition of Toxic IAPP Amyloid by Extracts of Common Fruits","volume":"12","author":"Kao P. Y.","year":"2015","journal-title":"Journal of Functional Foods"},{"key":"e_1_2_10_15_1","doi-asserted-by":"publisher","DOI":"10.2174\/1874091X01206010066"},{"key":"e_1_2_10_16_1","doi-asserted-by":"publisher","DOI":"10.3109\/13506129.2012.762761"},{"key":"e_1_2_10_17_1","doi-asserted-by":"publisher","DOI":"10.1021\/acs.biochem.5c00139"},{"key":"e_1_2_10_18_1","doi-asserted-by":"publisher","DOI":"10.3389\/fnut.2024.1408620"},{"key":"e_1_2_10_19_1","doi-asserted-by":"publisher","DOI":"10.1021\/acschemneuro.5c00269"},{"key":"e_1_2_10_20_1","doi-asserted-by":"publisher","DOI":"10.1002\/advs.202508344"},{"key":"e_1_2_10_21_1","doi-asserted-by":"publisher","DOI":"10.1039\/d5tb02851e"},{"key":"e_1_2_10_22_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.ijbiomac.2022.06.107"},{"key":"e_1_2_10_23_1","doi-asserted-by":"publisher","DOI":"10.2174\/0109298665340227241115110404"},{"key":"e_1_2_10_24_1","doi-asserted-by":"publisher","DOI":"10.1021\/acs.biochem.5b01107"},{"key":"e_1_2_10_25_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0909024107"},{"key":"e_1_2_10_26_1","doi-asserted-by":"publisher","DOI":"10.3390\/ijms21124287"},{"key":"e_1_2_10_27_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbapap.2022.140866"},{"key":"e_1_2_10_28_1","doi-asserted-by":"publisher","DOI":"10.1021\/Bi100337p"},{"issue":"5","key":"e_1_2_10_29_1","doi-asserted-by":"crossref","first-page":"872","DOI":"10.1021\/bi901751b","article-title":"The Ability of Rodent Islet Amyloid Polypeptide to Inhibit Amyloid Formation by Human Islet Amyloid Polypeptide Has Important Implications for the Mechanism of Amyloid Formation and the Design of Inhibitors","volume":"49","author":"Cao P.","year":"2010","journal-title":"Biochemistry"},{"key":"e_1_2_10_30_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.cell.2025.12.001"},{"key":"e_1_2_10_31_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.1213151"},{"key":"e_1_2_10_32_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M117.774893"},{"key":"e_1_2_10_33_1","doi-asserted-by":"publisher","DOI":"10.1002\/prot.24007"},{"key":"e_1_2_10_34_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi3014278"},{"key":"e_1_2_10_35_1","doi-asserted-by":"publisher","DOI":"10.1002\/anie.201504973"},{"key":"e_1_2_10_36_1","doi-asserted-by":"publisher","DOI":"10.1021\/acs.chemrestox.0c00416"},{"key":"e_1_2_10_37_1","doi-asserted-by":"publisher","DOI":"10.1002\/1873\u20103468.12261"},{"key":"e_1_2_10_38_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbagen.2009.02.013"},{"key":"e_1_2_10_39_1","doi-asserted-by":"publisher","DOI":"10.1007\/s13340\u2010018\u20100347\u20101"},{"key":"e_1_2_10_40_1","doi-asserted-by":"publisher","DOI":"10.1038\/s41467\u2010020\u201020454\u2010z"}],"container-title":["Journal of Peptide Science"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/pdf\/10.1002\/psc.70140","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/full-xml\/10.1002\/psc.70140","content-type":"application\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/pdf\/10.1002\/psc.70140","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,10,17]],"date-time":"2026-10-17T03:48:21Z","timestamp":1792208901000},"score":1,"resource":{"primary":{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/10.1002\/psc.70140"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,10,16]]},"references-count":39,"journal-issue":{"issue":"12","published-print":{"date-parts":[[2026,12]]}},"alternative-id":["10.1002\/psc.70140"],"URL":"https:\/\/doi.org\/10.1002\/psc.70140","archive":["Portico"],"relation":{},"ISSN":["1075-2617","1099-1387"],"issn-type":[{"value":"1075-2617","type":"print"},{"value":"1099-1387","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,10,16]]},"assertion":[{"value":"2026-07-11","order":0,"name":"received","label":"Received","group":{"name":"publication_history","label":"Publication History"}},{"value":"2026-10-08","order":2,"name":"accepted","label":"Accepted","group":{"name":"publication_history","label":"Publication History"}},{"value":"2026-10-16","order":3,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}],"article-number":"e70140"}}