<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Vijaya Kumar DK</submitter><funding>Cure Alzheimer's Fund</funding><funding>Cure Alzheimer&amp;apos;s Fund</funding><funding>Dake Family Foundation</funding><funding>National Institutes of Health</funding><funding>NIH HHS</funding><pagination>e70490</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC12307129</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>21(8)</volume><pubmed_abstract>&lt;h4>Introduction&lt;/h4>Our previous studies demonstrated the antimicrobial properties of amyloid beta (Aβ) of Alzheimer's disease (AD) against clinically relevant bacteria, yeast, and viruses. In this study, we investigate the antimicrobial function of the 37-amino acid amylin of type 2 diabetes (T2D), expanding on its potential involvement in AD.&lt;h4>Methods&lt;/h4>We used in vitro assays, including human three-dimensional neuronal cell culture models, to test microbicidal, microbiostatic, and synergistic antimicrobial interactions between amylin and Aβ against microbes.&lt;h4>Results&lt;/h4>Our results confirm that amylin is a broad-spectrum antimicrobial peptide that exhibits both microbicidal and microbiostatic mechanisms. We also identified a synergistic antimicrobial effect between amylin and Aβ</pubmed_abstract><journal>Alzheimer's &amp; dementia : the journal of the Alzheimer's Association</journal><pubmed_title>Human amylin is a potent antimicrobial peptide that exhibits antimicrobial synergism with the amyloid beta protein.</pubmed_title><pmcid>PMC12307129</pmcid><funding_grant_id>238023</funding_grant_id><funding_grant_id>1S10RR023594S10</funding_grant_id><pubmed_authors>Mitchell TA</pubmed_authors><pubmed_authors>Moir AP</pubmed_authors><pubmed_authors>Su C</pubmed_authors><pubmed_authors>Moir RD</pubmed_authors><pubmed_authors>Kim E</pubmed_authors><pubmed_authors>Navalpur Shanmugam NK</pubmed_authors><pubmed_authors>Choi SH</pubmed_authors><pubmed_authors>Rodriguez AS</pubmed_authors><pubmed_authors>Vijaya Kumar DK</pubmed_authors><pubmed_authors>Eimer WA</pubmed_authors><pubmed_authors>Tanzi RE</pubmed_authors><pubmed_authors>Tailor BA</pubmed_authors><pubmed_authors>Ghelichi J</pubmed_authors></additional><is_claimable>false</is_claimable><name>Human amylin is a potent antimicrobial peptide that exhibits antimicrobial synergism with the amyloid beta protein.</name><description>&lt;h4>Introduction&lt;/h4>Our previous studies demonstrated the antimicrobial properties of amyloid beta (Aβ) of Alzheimer's disease (AD) against clinically relevant bacteria, yeast, and viruses. In this study, we investigate the antimicrobial function of the 37-amino acid amylin of type 2 diabetes (T2D), expanding on its potential involvement in AD.&lt;h4>Methods&lt;/h4>We used in vitro assays, including human three-dimensional neuronal cell culture models, to test microbicidal, microbiostatic, and synergistic antimicrobial interactions between amylin and Aβ against microbes.&lt;h4>Results&lt;/h4>Our results confirm that amylin is a broad-spectrum antimicrobial peptide that exhibits both microbicidal and microbiostatic mechanisms. We also identified a synergistic antimicrobial effect between amylin and Aβ</description><dates><release>2025-01-01T00:00:00Z</release><publication>2025 Aug</publication><modification>2026-03-27T15:28:59.599Z</modification><creation>2025-08-24T03:07:16.324Z</creation></dates><accession>S-EPMC12307129</accession><cross_references><pubmed>40731182</pubmed><doi>10.1002/alz.70490</doi></cross_references></HashMap>