{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,4]],"date-time":"2026-09-04T05:02:12Z","timestamp":1788498132419,"version":"build-2803163510"},"reference-count":28,"publisher":"SAGE Publications","issue":"1","license":[{"start":{"date-parts":[[2012,2,1]],"date-time":"2012-02-01T00:00:00Z","timestamp":1328054400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.sagepub.com\/page\/policies\/text-and-data-mining-license"}],"content-domain":{"domain":["journals.sagepub.com"],"crossmark-restriction":true},"short-container-title":["Eur J Mass Spectrom (Chichester)"],"published-print":{"date-parts":[[2012,2]]},"abstract":"<jats:p>\n                    The metal ion binding sites of human islet amyloid polypeptide (hIAPP) have been investigated to explain the biological activity difference in the fibril formation process. The structures of [hIAPP\u1e6bCu (or Al)]\n                    <jats:sup>n+<\/jats:sup>\n                    and [hIAPP\n                    <jats:sub>17\u201330<\/jats:sub>\n                    \u1e6bCu]\n                    <jats:sup>2+<\/jats:sup>\n                    complex were investigated by electrospray ionization\u2013mass spectrometry (ESI-MS). The fragmentation patterns of [hIAPP\u1e6bCu (or Al)]\n                    <jats:sup>n+<\/jats:sup>\n                    and [hIAPP\n                    <jats:sub>17\u201330<\/jats:sub>\n                    \u1e6bCu]\n                    <jats:sup>2+<\/jats:sup>\n                    complex were analyzed by tandem mass spectrometry (MS\/MS) and multi-stage mass spectrometry (MS\n                    <jats:sup>3<\/jats:sup>\n                    ) spectra. The [hIAPP+Cu+H]\n                    <jats:sup>3+<\/jats:sup>\n                    , [hIAPP+Al+H]\n                    <jats:sup>4+<\/jats:sup>\n                    and [hIAPP\n                    <jats:sub>17\u201330<\/jats:sub>\n                    +Cu]\n                    <jats:sup>2+<\/jats:sup>\n                    complexes were observed in MS spectra. The Cu binding site of hIAPP is suggested to be the N\n                    <jats:sub>22<\/jats:sub>\n                    \u2013F\u2013G\u2013A\u2013I\n                    <jats:sub>26<\/jats:sub>\n                    part for the [hIAPP+Cu+H]\n                    <jats:sup>3+<\/jats:sup>\n                    gas-phase complex. The original hIAPP conformation was supposed to be changed by the interaction between the Cu ion and the N\n                    <jats:sub>22<\/jats:sub>\n                    \u2013F\u2013G\u2013A\u2013I\n                    <jats:sub>26<\/jats:sub>\n                    part in the [hIAPP+Cu+H]\n                    <jats:sup>3+<\/jats:sup>\n                    gas-phase complex.\n                  <\/jats:p>","DOI":"10.1255\/ejms.1167","type":"journal-article","created":{"date-parts":[[2012,3,26]],"date-time":"2012-03-26T11:10:12Z","timestamp":1332760212000},"page":"51-58","update-policy":"https:\/\/doi.org\/10.1177\/sage-journals-update-policy","source":"Crossref","is-referenced-by-count":10,"title":["Investigation of the Copper Binding Site on the Human Islet Amyloid Polypeptide Hormone"],"prefix":"10.1177","volume":"18","author":[{"given":"Mi-Ji","family":"Kim","sequence":"first","affiliation":[{"name":"Department of Applied Chemistry, Kumoh National Institute of Technology, 1 Yangho-Dong, Gumi, Republic of Korea, 730-701"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ho-Tae","family":"Kim","sequence":"additional","affiliation":[{"name":"Department of Applied Chemistry, Kumoh National Institute of Technology, 1 Yangho-Dong, Gumi, Republic of Korea, 730-701"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"179","published-online":{"date-parts":[[2012,2,1]]},"reference":[{"key":"bibr1-ejms.1167","doi-asserted-by":"publisher","DOI":"10.1016\/S0006-3495(03)74996-0"},{"key":"bibr2-ejms.1167","doi-asserted-by":"publisher","DOI":"10.1016\/j.biocel.2005.12.009"},{"key":"bibr3-ejms.1167","doi-asserted-by":"publisher","DOI":"10.1038\/368756a0"},{"key":"bibr4-ejms.1167","doi-asserted-by":"publisher","DOI":"10.1016\/S1074-5521(00)00034-X"},{"key":"bibr5-ejms.1167","doi-asserted-by":"publisher","DOI":"10.1016\/j.jinorgbio.2010.05.012"},{"key":"bibr6-ejms.1167","volume-title":"Amylin: Physiology and Pharmacology.","author":"Young 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