{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,24]],"date-time":"2026-03-24T04:31:49Z","timestamp":1774326709608,"version":"3.50.1"},"reference-count":51,"publisher":"Wiley","issue":"10","license":[{"start":{"date-parts":[[2020,9,6]],"date-time":"2020-09-06T00:00:00Z","timestamp":1599350400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["81873193, 21904022 and 21673219"],"award-info":[{"award-number":["81873193, 21904022 and 21673219"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["analyticalsciencejournals.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["J Mass Spectrom"],"published-print":{"date-parts":[[2020,10]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>A wealth of epidemiological evidence indicates a strong link between type 2 diabetes (T2D) and Alzheimer's disease (AD). The fiber deposition with cross\u2010\u03b2\u2010sheet structure formed by self\u2010aggregation and misfolding of amyloidogenic peptides is a common hallmark of both diseases. For the patients with T2D, the fibrils are mainly found in the islets of Langerhans that results from the accumulation of human islet amyloid polypeptide (hIAPP). The major component of aggregates located in the brain of AD patients is amyloid\u2010\u03b2 (A\u03b2). Many biophysical and physiological properties are shared by hIAPP and A\u03b2, and both peptides show similar cytotoxic mechanisms. Therefore, it is meaningful to investigate the possible cross\u2010interactions of hIAPP and A\u03b2 in both diseases. In this article, the segment 25\u201335 of A\u03b2 was selected because A\u03b2<jats:sub>25\u201335<\/jats:sub> was a core region in the process of amyloid formation and showed similar aggregation tendency and toxicity with full\u2010length A\u03b2. The electrospray ionization\u2010ion mobility\u2010mass spectrometry analysis and thioflavin T fluorescence kinetic analysis combined with transmission electron microscopy were used to explore the effects of the coexistence of A\u03b2<jats:sub>25\u201335<\/jats:sub> and hIAPP on the self\u2010aggregation of both peptides and whether there was co\u2010assembly in fibrillation. The results indicated that the aggregation of hIAPP and A\u03b2<jats:sub>25\u201335<\/jats:sub> had two nucleation stages in the binary mixtures. hIAPP and A\u03b2<jats:sub>25\u201335<\/jats:sub> had a high binding affinity and a series of hetero\u2010oligomers formed in the mixtures of hIAPP and A\u03b2<jats:sub>25\u201335<\/jats:sub> in the early stage. The cross\u2010reaction between hIAPP monomers and A\u03b2<jats:sub>25\u201335<\/jats:sub> monomers as well as a little of oligomers during primary nucleation stage could accelerate the aggregation of A\u03b2<jats:sub>25\u201335<\/jats:sub>. However, owing to the obvious difference in aggregation ability between hIAPP and A\u03b2<jats:sub>25\u201335<\/jats:sub>, this cross\u2010interaction had no significant impact on the self\u2010assembly of hIAPP. Our study may offer a better understanding for exploring the molecular mechanism of the association between AD and T2D observed in clinical and epidemiological studies and developing therapeutic strategies against amyloid diseases.<\/jats:p>","DOI":"10.1002\/jms.4643","type":"journal-article","created":{"date-parts":[[2020,8,10]],"date-time":"2020-08-10T22:39:46Z","timestamp":1597099186000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["Studies on the cross\u2010interaction between hIAPP and A\u03b2<sub>25\u201335<\/sub> and the aggregation process in binary mixture by electrospray ionization\u2010ion mobility\u2010mass spectrometry"],"prefix":"10.1002","volume":"55","author":[{"given":"Bo","family":"Pang","sequence":"first","affiliation":[{"name":"State Key Laboratory of Electroanalytical Chemistry, National Center of Mass Spectrometry in Changchun, Jilin Province Key Laboratory of Chinese Medicine Chemistry and 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