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The two hormones act in different ways: in fact insulin triggers glucose uptake in muscle and liver cells, removing glucose from the bloodstream and making it available for energy use and storage, while amylin regulates glucose homeostasis. Aside these positive physiological aspects, human amyloid polypeptide (hIAPP) readily forms amyloid <jats:italic>in vitro<\/jats:italic>. Amyloids are aggregates of proteins and in the human body amyloids are considered responsible of the development of various diseases. These aspects have been widely described and discussed in literature and to give a view of the highly complexity of this biochemical behavior the different physical, chemical, biological and medical aspects are shortly described in this review. It is strongly affected by the presence on metal ions, responsible for or inhibiting the formation of fibrils. Mass spectrometry resulted (and still results) to be a particularly powerful tool to obtain valid and effective experimental data to describe the hIAPP behavior. Aside classical approaches devoted to investigation on metal ion\u2010hIAPP structures, which reflects on the identification of metal\u2013protein interaction site(s) and of possible metal\u2010induced conformational changes of the protein, interesting results have been obtained by ion mobility mass spectrometry, giving, on the basis of collisional cross\u2010section data, information on both the oligomerization processes and the conformation changes. Laser ablation electrospray ionization\u2014ion mobility spectrometry\u2010mass spectrometry (LAESI\u2010IMS\u2010MS), allowed to obtain information on the binding stoichiometry, complex dissociation constant, and the oxidation state of the copper for the amylin\u2013copper interaction. Alternatively to inorganic ions, small organic molecules have been tested by ESI\u2010IMS\u2010MS as inhibitor of amyloid assembly. Also in this case the obtained data demonstrate the validity of the ESI\u2010IMS\u2010MS approach as a high\u2010throughput screen for inhibitors of amyloid assembly, providing valid information concerning the identity of the interacting species, the nature of binding and the effect of the ligand on protein aggregation. Effects of Cu<jats:sup>2+<\/jats:sup> and Zn<jats:sup>2+<\/jats:sup> ions in the degradation of human and murine IAPP by insulin\u2010degrading enzyme were studied by liquid chromatography\/mass spectrometry (LC\/MS). The literature data show that mass spectrometry is a highly valid and effective tool in the study of the amylin behavior, so to individuate medical strategies to avoid the undesired formation of amyloids in <jats:italic>in vivo<\/jats:italic> conditions.<\/jats:p>","DOI":"10.1002\/mas.21732","type":"journal-article","created":{"date-parts":[[2021,9,24]],"date-time":"2021-09-24T19:01:28Z","timestamp":1632510088000},"page":"984-1007","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":5,"title":["Role of mass spectrometry in the study of interactions between amylin and metal ions"],"prefix":"10.1002","volume":"42","author":[{"given":"Laura","family":"Moracci","sequence":"first","affiliation":[{"name":"Department of Surgical, Oncological and Gastroenterological Sciences University of Padova Padova Italy"},{"name":"Fondazione Istituto di Ricerca Pediatrica Citt\u00e0 della Speranza Padova Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sara","family":"Crotti","sequence":"additional","affiliation":[{"name":"Department of Surgical, Oncological and Gastroenterological Sciences University of Padova Padova Italy"},{"name":"Fondazione Istituto di Ricerca Pediatrica Citt\u00e0 della Speranza Padova Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pietro","family":"Traldi","sequence":"additional","affiliation":[{"name":"Fondazione Istituto di Ricerca Pediatrica Citt\u00e0 della Speranza Padova Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marco","family":"Agostini","sequence":"additional","affiliation":[{"name":"Department of Surgical, Oncological and Gastroenterological Sciences University of Padova Padova Italy"},{"name":"Fondazione Istituto di Ricerca Pediatrica Citt\u00e0 della Speranza Padova Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chiara","family":"Cosma","sequence":"additional","affiliation":[{"name":"Department of Medicine University of Padova Padova Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Annunziata","family":"Lapolla","sequence":"additional","affiliation":[{"name":"Department of Medicine University of Padova Padova Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2021,9,24]]},"reference":[{"key":"e_1_2_6_2_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.neurobiolaging.2013.10.076"},{"key":"e_1_2_6_3_1","doi-asserted-by":"publisher","DOI":"10.1155\/2016\/2798269"},{"key":"e_1_2_6_4_1","doi-asserted-by":"publisher","DOI":"10.1021\/acs.inorgchem.9b03498"},{"key":"e_1_2_6_5_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.jinorgbio.2018.11.004"},{"key":"e_1_2_6_6_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.jalz.2016.03.001"},{"key":"e_1_2_6_7_1","doi-asserted-by":"publisher","DOI":"10.1002\/jms.3338"},{"key":"e_1_2_6_8_1","doi-asserted-by":"publisher","DOI":"10.1111\/bph.13496"},{"key":"e_1_2_6_9_1","doi-asserted-by":"publisher","DOI":"10.1021\/ja1007867"},{"key":"e_1_2_6_10_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.febslet.2013.01.046"},{"key":"e_1_2_6_11_1","doi-asserted-by":"publisher","DOI":"10.1039\/C9MT00236G"},{"key":"e_1_2_6_12_1","doi-asserted-by":"publisher","DOI":"10.1210\/edrv-15-2-163"},{"key":"e_1_2_6_13_1","doi-asserted-by":"publisher","DOI":"10.1021\/ja903814q"},{"key":"e_1_2_6_14_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M111.331181"},{"key":"e_1_2_6_15_1","doi-asserted-by":"publisher","DOI":"10.1210\/jc.2017-02265"},{"key":"e_1_2_6_16_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0006-291X(84)80190-4"},{"key":"e_1_2_6_17_1","doi-asserted-by":"publisher","DOI":"10.1006\/jsbi.2000.4268"},{"key":"e_1_2_6_18_1","doi-asserted-by":"publisher","DOI":"10.1007\/s00775-019-01637-6"},{"key":"e_1_2_6_19_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.jinorgbio.2018.08.012"},{"key":"e_1_2_6_20_1","doi-asserted-by":"publisher","DOI":"10.29245\/2572.942X\/2019\/1.1212"},{"key":"e_1_2_6_21_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.1566067"},{"key":"e_1_2_6_22_1","doi-asserted-by":"publisher","DOI":"10.1124\/pr.115.010629"},{"issue":"4","key":"e_1_2_6_23_1","first-page":"124","article-title":"\u201cA\u201d is for amylin and amyloid in Type 2 diabetes mellitus","volume":"2","author":"Hayden MR","year":"2001","journal-title":"JOP. 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