{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,3]],"date-time":"2026-08-03T18:55:09Z","timestamp":1785783309092,"version":"3.56.0"},"reference-count":85,"publisher":"SAGE Publications","issue":"1","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["JAD"],"published-print":{"date-parts":[[2022,5,3]]},"abstract":"<jats:p>Background: Type 2 diabetes related human islet amyloid polypeptide (hIAPP) plays a dual role in Alzheimer\u2019s disease (AD). hIAPP has neuroprotective effects in AD mouse models whereas, high hIAPP concentrations can promote co-aggregation with amyloid-\u03b2 (A\u03b2) to promote neurodegeneration. In fact, both low and high plasma hIAPP concentration has been associated with AD. Therefore, non-aggregating hIAPP analogues have garnered interest as a treatment for AD. The aromatic amino acids F23 and I26 in hIAPP have been identified as the key residues involved in self-aggregation and A\u03b2 cross-seeding. Objective: Three novel IAPP analogues with single and double alanine mutations (A1\u200a=\u200aF23, A2\u200a=\u200aI26, and A3\u200a=\u200aF23\u200a+\u200aI26) were assessed for their ability to aggregate, modulate A\u03b2 oligomer formation, and alter neurotoxicity. Methods: A range of biophysical methods including Thioflavin-T, gel electrophoresis, photo-crosslinking, circular dichroism combined with cell viability assays were utilized to assess protein aggregation and toxicity. Results: All IAPP analogues showed significantly less self-aggregation than hIAPP. Co-aggregated A\u03b242-A2 and A3 also showed reduced aggregation compared to A\u03b242-hIAPP mixtures. Self- and co-oligomerized A1, A2, and A3 exhibited random coil conformations with reduced beta sheet content compared to hIAPP and A\u03b242-hIAPP aggregates. A1 was toxic at high concentrations compared to A2 and A3. However, co-aggregated A\u03b242-A1, A2, or A3 showed reduced neurotoxicity compared to A\u03b242, hIAPP, and A\u03b242-hIAPP aggregates. Conclusion: These findings confirm that hIAPP analogues with non-aromatic residues at positions 23 and 26 have reduced self-aggregation and the ability to neutralize A\u03b242 toxicity. This warrants further characterization of their protective effects in pre-clinical AD models.<\/jats:p>","DOI":"10.3233\/jad-215339","type":"journal-article","created":{"date-parts":[[2022,3,11]],"date-time":"2022-03-11T11:52:53Z","timestamp":1646999573000},"page":"373-390","source":"Crossref","is-referenced-by-count":8,"title":["Novel Amylin Analogues Reduce Amyloid-\u03b2 Cross-Seeding Aggregation and Neurotoxicity"],"prefix":"10.1177","volume":"87","author":[{"given":"Gowdame Lakshmanan","family":"Dharmaraj","sequence":"first","affiliation":[{"name":"Curtin Medical School, Curtin Health Innovation Research Institute, Curtin University, Perth, WA, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fraulein Denise","family":"Arigo","sequence":"additional","affiliation":[{"name":"Curtin Medical School, Curtin Health Innovation Research Institute, Curtin University, Perth, WA, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kimberly A.","family":"Young","sequence":"additional","affiliation":[{"name":"Curtin Medical School, Curtin Health Innovation Research Institute, Curtin University, Perth, WA, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ralph","family":"Martins","sequence":"additional","affiliation":[{"name":"Centre of Excellence for Alzheimer\u2019s Disease Research and Care, School of Medical and Health Sciences, Edith Cowan University, Perth, WA, Australia"},{"name":"School of Biomedical Science, Macquarie University, Sydney, NSW, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ricardo L.","family":"Mancera","sequence":"additional","affiliation":[{"name":"Curtin Medical School, Curtin Health Innovation Research Institute, Curtin University, Perth, WA, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Prashant","family":"Bharadwaj","sequence":"additional","affiliation":[{"name":"Curtin Medical School, Curtin Health Innovation 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