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Substantial effort has gone into developing inhibitors, particularly short peptides, capable of targeting hIAPP and disrupting its amyloidogenic process, offering potential therapeutic strategies to prevent or slow T2D progression. Here, we demonstrate the effectiveness of the anti\u2010amyloidogenic peptide QBP1 in halting the conformational conversion of hIAPP into \u03b2\u2010structured aggregates, thereby preventing amyloidogenesis and its associated cytotoxicity. First, we evaluated the anti\u2010amyloidogenic effects of QBP1 through cell\u2010free in vitro aggregation experiments, including Thioflavin\u2010T fluorescence, A11\/OC dot blotting, and negative\u2010stain electron microscopy. Circular dichroism and nuclear magnetic resonance spectroscopy corroborated that QBP1 delays hIAPP \u03b2\u2010sheet formation and oligomerization, respectively, with an efficacy comparable to that of epigallocatechin\u20103\u2010gallate. Second, we performed cell\u2010based in vitro experiments to investigate cytoprotection in INS\u20101E \u03b2\u2010cells by fusing QBP1 to the cell\u2010penetrating peptide penetratin (\n                    <jats:italic>Antp<\/jats:italic>\n                    \u2010QBP1). Viability assays, immunocytochemistry, and gene expression analysis showed that under amyloidogenic stress\n                    <jats:italic>Antp<\/jats:italic>\n                    \u2010QBP1 preserves \u03b2\u2010cell viability and metabolic homeostasis by preventing the formation of early toxic hIAPP intermediates. Finally, in silico experiments using molecular dynamics simulations revealed stable QBP1\u2013hIAPP interactions mediated by van der Waals forces and \u03c0\u2013H contacts involving hydrophobic and aromatic residues (e.g., W, F), supported by favorable non\u2010polar solvation and structural complementarity. Taken together, these findings identify QBP1 as a promising candidate for strategies aimed at reducing islet amyloid burden and preserving \u03b2\u2010cell integrity in T2D.\n                  <\/jats:p>","DOI":"10.1002\/advs.202508344","type":"journal-article","created":{"date-parts":[[2026,4,22]],"date-time":"2026-04-22T10:05:03Z","timestamp":1776852303000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":2,"title":["QBP1 Peptide as a Potential Anti\u2010Amyloidogenic Therapy for Type 2 Diabetes: An In Vitro Study"],"prefix":"10.1002","volume":"13","author":[{"given":"Mar\u00eda M.","family":"Tejero\u2010Ojeda","sequence":"first","affiliation":[{"name":"Instituto Cajal Consejo Superior de Investigaciones Cient\u00edficas (CSIC)  Madrid Spain"},{"name":"PhD Program in Neuroscience Universidad Aut\u00f3noma de Madrid\u2010Cajal Institute  Madrid Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ada 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