{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,4]],"date-time":"2026-09-04T05:02:54Z","timestamp":1788498174398,"version":"build-2803163510"},"reference-count":66,"publisher":"American Chemical Society (ACS)","issue":"4","license":[{"start":{"date-parts":[[2020,2,17]],"date-time":"2020-02-17T00:00:00Z","timestamp":1581897600000},"content-version":"vor","delay-in-days":11,"URL":"https:\/\/pubs.acs.org\/page\/policy\/authorchoice_termsofuse.html"}],"funder":[{"DOI":"10.13039\/na","name":"M.A., A-H.E., \u00c5&#x81;.J. and M.J. would like to thank King Abdullah University of Science and Technology (KAUST) for the financial support","doi-asserted-by":"publisher","award":["NA"],"award-info":[{"award-number":["NA"]}],"id":[{"id":"10.13039\/na","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2020,2,17]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Protein aggregation has attracted substantial interest because of its role in causing many serious illnesses, such as neurodegenerative diseases and type II diabetes. Recent studies have shown that protein aggregation can be prevented by forming metal ion complexes with a target protein, which affects their conformation in solution and their physical properties, such as aggregation. Thus, understanding the interactions between aggregating molecules and bioactive metal ions such as Cu2+ is beneficial for new drug discovery. Pramlintide, a synthetic peptide drug, and its natural counterpart rat amylin are known to be resistant to aggregation because of the presence of proline residues, which are usually \u03b2-sheet \u201cbreakers\u201d within their amino acid sequence. Here, we investigate the Cu2+ coordination properties of pramlintide and rat amylin using nuclear magnetic resonance, circular dichroism, electron paramagnetic resonance, ultraviolet\u2013visible spectroscopy, potentiometry, and mass spectrometry. We test the influence of Cu2+ on the aggregation properties of these amylin analogues with thioflavin T assays. We find that both peptides form stable complexes with Cu2+ with similar affinities at a 1:1 ratio. The N-termini of both peptides are involved in Cu2+ binding; His18 imidazole is an equally attractive binding site in the case of pramlintide. Our results show that Cu2+ ions influence the aggregation of pramlintide, but not that of rat amylin.<\/jats:p>","DOI":"10.1021\/acs.inorgchem.9b03498","type":"journal-article","created":{"date-parts":[[2020,2,6]],"date-time":"2020-02-06T09:11:56Z","timestamp":1580980316000},"page":"2527-2535","source":"Crossref","is-referenced-by-count":27,"title":["Copper(II) and Amylin Analogues: A Complicated Relationship"],"prefix":"10.1021","volume":"59","author":[{"given":"Mawadda","family":"Alghrably","sequence":"first","affiliation":[{"name":"King Abdullah University of Science and Technology (KAUST) , , ,","place":["Thuwal, Saudi Arabia, 23955-6900"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dorota","family":"Dudek","sequence":"additional","affiliation":[{"name":"University of Wroclaw , , F. Joliot-Curie 14 , ,","place":["Wroclaw, Poland, 50383"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Abdul-Hamid","family":"Emwas","sequence":"additional","affiliation":[{"name":"King Abdullah University of Science and Technology (KAUST) , , ,","place":["Thuwal, Kingdom of Saudi Arabia, 23955"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"\u0141ukasz","family":"Jaremko","sequence":"additional","affiliation":[{"name":"King Abdullah University of Science and Technology (KAUST) , , ,","place":["Thuwal, Saudi Arabia, 23955-6900"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mariusz","family":"Jaremko","sequence":"additional","affiliation":[{"name":"King Abdullah University of Science and Technology (KAUST) , , ,","place":["Thuwal, Saudi Arabia, 23955-6900"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0425-1128","authenticated-orcid":true,"given":"Magdalena","family":"Rowin\u0301ska-Z\u0307yrek","sequence":"additional","affiliation":[{"name":"University of Wroclaw , , F. Joliot-Curie 14 , ,","place":["Wroclaw, Poland, 50383"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2020,2,6]]},"reference":[{"issue":"3","key":"2026090303525518300_cit1","doi-asserted-by":"publisher","first-page":"685","DOI":"10.1016\/j.bpj.2010.09.070","article-title":"Biphasic effects\nof insulin on islet amyloid polypeptide membrane disruption","volume":"100","author":"Brender","year":"2011","journal-title":"Biophys. 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Res."},{"issue":"4","key":"2026090303525518300_cit5","first-page":"554","article-title":"\"Texts\nand Documents\u201c: Banting\u2019s, Best\u2019s, and Collip\u2019s\nAccounts of the Discovery of Insulin","volume":"56","author":"Bliss","year":"1982","journal-title":"Bull.\nHist. Med."},{"key":"2026090303525518300_cit6","first-page":"93","article-title":"The discovery of insulin: the inside\nstory","volume":"16","author":"Bliss","year":"1997","journal-title":"Publ. - Am. Inst. Hist. Pharm."},{"issue":"3","key":"2026090303525518300_cit7","doi-asserted-by":"publisher","first-page":"795","DOI":"10.1152\/physrev.00042.2009","article-title":"Islet amyloid polypeptide, islet amyloid, and diabetes\nmellitus","volume":"91","author":"Westermark","year":"2011","journal-title":"Physiol. 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Biol."},{"issue":"S1994A","key":"2026090303525518300_cit11","doi-asserted-by":"publisher","first-page":"19","DOI":"10.1002\/jcb.240550004","article-title":"Molecular physiology of amylin","volume":"55","author":"Pittner","year":"1994","journal-title":"J. Cell. Biochem."},{"issue":"4","key":"2026090303525518300_cit12","doi-asserted-by":"publisher","first-page":"317","DOI":"10.2174\/187152208787169189","article-title":"Amylin-based pharmacotherapy-past,\npresent & future","volume":"8","author":"Roth","year":"2008","journal-title":"Immunol., Endocr. Metab.\nAgents Med. Chem."},{"issue":"10","key":"2026090303525518300_cit13","doi-asserted-by":"publisher","first-page":"1500","DOI":"10.1016\/j.clinthera.2005.10.009","article-title":"Pramlintide in the\ntreatment of type 1 and type 2 diabetes mellitus","volume":"27","author":"Ryan","year":"2005","journal-title":"Clin. 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Biochem."},{"key":"2026090303525518300_cit22","doi-asserted-by":"publisher","first-page":"69","DOI":"10.1016\/j.jinorgbio.2018.11.004","article-title":"Interaction of amylin species with transition metals\nand membranes","volume":"191","author":"Alghrably","year":"2019","journal-title":"J. Inorg. Biochem."},{"issue":"37","key":"2026090303525518300_cit23","doi-asserted-by":"publisher","first-page":"6909","DOI":"10.1039\/c0cc02141e","article-title":"Copper-induced cytotoxicity:\nreactive oxygen species or islet amyloid polypeptide oligomer formation","volume":"46","author":"Yu","year":"2010","journal-title":"Chem. Commun. (Cambridge, U. K.)"},{"key":"2026090303525518300_cit24","doi-asserted-by":"publisher","first-page":"143","DOI":"10.1016\/j.jinorgbio.2014.07.002","article-title":"Cu(II) inhibits hIAPP fibrillation\nand promotes hIAPP-induced beta cell apoptosis through induction of\nROS-mediated mitochondrial dysfunction","volume":"140","author":"Ma","year":"2014","journal-title":"J. Inorg.\nBiochem."},{"key":"2026090303525518300_cit25","doi-asserted-by":"publisher","first-page":"215","DOI":"10.1039\/C9RA09350H","article-title":"Aggregation of biologically important peptides and\nproteins: inhibition or acceleration depending on protein and metal\nion concentrations","volume":"10","author":"Poulson","year":"2020","journal-title":"RSC Adv."},{"issue":"35","key":"2026090303525518300_cit26","doi-asserted-by":"publisher","first-page":"27986","DOI":"10.1039\/C4RA13315C","article-title":"Free radicals, natural antioxidants, and their reaction mechanisms","volume":"5","author":"Nimse","year":"2015","journal-title":"RSC Adv."},{"issue":"19","key":"2026090303525518300_cit27","doi-asserted-by":"publisher","first-page":"9829","DOI":"10.1021\/acs.analchem.5b02217","article-title":"Rapid Assessment of Human Amylin\nAggregation and Its Inhibition by Copper(II) Ions by Laser Ablation\nElectrospray Ionization Mass Spectrometry with Ion Mobility Separation","volume":"87","author":"Li","year":"2015","journal-title":"Anal. 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Acta"},{"issue":"39","key":"2026090303525518300_cit31","doi-asserted-by":"publisher","first-page":"17091","DOI":"10.1039\/C5DT02445E","article-title":"Potentiometric\nand spectroscopic studies on the copper (II) complexes of rat amylin\nfragments. The anchoring ability of specific non-coordinating side\nchains","volume":"44","author":"Da\u0301vid","year":"2015","journal-title":"Dalton Transactions"},{"issue":"20","key":"2026090303525518300_cit32","doi-asserted-by":"publisher","first-page":"10727","DOI":"10.1021\/acs.inorgchem.6b01963","article-title":"Copper coordination\nfeatures of human islet amyloid polypeptide: the type 2 diabetes peptide","volume":"55","author":"Sa\u0301nchez-Lo\u0301pez","year":"2016","journal-title":"Inorg. Chem."},{"issue":"19","key":"2026090303525518300_cit33","doi-asserted-by":"publisher","first-page":"8099","DOI":"10.1039\/C6DT00628K","article-title":"Coordination\nof Zn 2+ and Cu 2+ to the membrane disrupting fragment of amylin","volume":"45","author":"Rowin\u0301ska-Z\u0307yrek","year":"2016","journal-title":"Dalton Transactions"},{"issue":"71","key":"2026090303525518300_cit34","doi-asserted-by":"publisher","first-page":"17898","DOI":"10.1002\/chem.201704910","article-title":"From peptide\nfragments to whole protein: copper (II) load and coordination features\nof IAPP","volume":"23","author":"Magri\u0300","year":"2017","journal-title":"Chem. - Eur. J."},{"issue":"4","key":"2026090303525518300_cit35","doi-asserted-by":"publisher","first-page":"559","DOI":"10.3891\/acta.chem.scand.04-0559","article-title":"Determination of the equivalent point\nin potentiometric titrations","volume":"4","author":"Gran","year":"1950","journal-title":"Acta Chem. Scand."},{"issue":"6","key":"2026090303525518300_cit36","doi-asserted-by":"publisher","first-page":"1195","DOI":"10.1039\/dt9850001195","article-title":"SUPERQUAD: an improved general program\nfor computation of formation constants from potentiometric data","author":"Gans","year":"1985","journal-title":"J. Chem. Soc., Dalton Trans."},{"issue":"10","key":"2026090303525518300_cit37","doi-asserted-by":"publisher","first-page":"1739","DOI":"10.1016\/0039-9140(96)01958-3","article-title":"Investigation\nof equilibria in solution. Determination of equilibrium constants\nwith the HYPERQUAD suite of programs","volume":"43","author":"Gans","year":"1996","journal-title":"Talanta"},{"issue":"1","key":"2026090303525518300_cit38","doi-asserted-by":"publisher","first-page":"311","DOI":"10.1016\/S0010-8545(98)00260-4","article-title":"Hyperquad simulation and speciation (HySS): a utility program for\nthe investigation of equilibria involving soluble and partially soluble\nspecies","volume":"184","author":"Alderighi","year":"1999","journal-title":"Coord. Chem. Rev."},{"issue":"4","key":"2026090303525518300_cit39","doi-asserted-by":"publisher","first-page":"700","DOI":"10.1021\/ac60260a013","article-title":"Use of the glass electrode in deuterium oxide and the\nrelation between the standardized pD (paD) scale and the operational\npH in heavy water","volume":"40","author":"Covington","year":"1968","journal-title":"Anal. Chem."},{"issue":"3","key":"2026090303525518300_cit40","doi-asserted-by":"publisher","first-page":"277","DOI":"10.1007\/BF00197809","article-title":"NMRPipe: a multidimensional spectral\nprocessing system based on UNIX pipes","volume":"6","author":"Delaglio","year":"1995","journal-title":"J. Biomol.\nNMR"},{"key":"2026090303525518300_cit41","volume-title":"Sparky 3","author":"Goddard","year":"2008"},{"issue":"1","key":"2026090303525518300_cit42","doi-asserted-by":"publisher","first-page":"11","DOI":"10.1051\/epn\/19861701011","article-title":"NMR with proteins\nand nucleic acids","volume":"17","author":"Wu\u0308thrich","year":"1986","journal-title":"Europhys. 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Mater."},{"key":"2026090303525518300_cit46","doi-asserted-by":"publisher","first-page":"155","DOI":"10.1016\/j.nanoen.2018.04.032","article-title":"Phosphine\nplasma activation of alpha-Fe2O3 for high energy asymmetric supercapacitors","volume":"49","author":"Liang","year":"2018","journal-title":"Nano Energy"},{"issue":"46","key":"2026090303525518300_cit47","doi-asserted-by":"publisher","first-page":"13655","DOI":"10.1021\/jp308423x","article-title":"Mn2+-Nucleotide Coordination at the\nMyosin Active Site As Detected by Pulsed Electron Paramagnetic Resonance","volume":"116","author":"Astashkin","year":"2012","journal-title":"J. Phys. Chem. B"},{"issue":"1\u20134","key":"2026090303525518300_cit48","doi-asserted-by":"publisher","first-page":"257","DOI":"10.1007\/s00723-009-0095-2","article-title":"EPR Spectra of Transition-Metal Proteins:\nthe Benefits of Data Deposition in Standard Formats","volume":"37","author":"Cammack","year":"2010","journal-title":"Appl. Magn. Reson."},{"issue":"11","key":"2026090303525518300_cit49","doi-asserted-by":"publisher","first-page":"1146","DOI":"10.1021\/ar200014u","article-title":"The Heterogeneous\nNature of Cu2+ Interactions with Alzheimer\u2019s Amyloid-beta Peptide","volume":"44","author":"Drew","year":"2011","journal-title":"Acc. Chem. Res."},{"issue":"41","key":"2026090303525518300_cit50","doi-asserted-by":"publisher","first-page":"13214","DOI":"10.1021\/bi049525k","article-title":"High-affinity metal-binding site in beef heart mitochondrial\nF(1)ATPase: An EPR spectroscopy study","volume":"43","author":"Zoleo","year":"2004","journal-title":"Biochemistry"},{"issue":"5\u20136","key":"2026090303525518300_cit51","doi-asserted-by":"publisher","first-page":"724","DOI":"10.1016\/S0009-2614(02)01845-6","article-title":"A tuneable\ndoubly stacked dielectric resonator housed in an intact TE102 cavity\nfor electron paramagnetic resonance spectroscopy","volume":"368","author":"Mattar","year":"2003","journal-title":"Chem. Phys. Lett."},{"issue":"52","key":"2026090303525518300_cit52","doi-asserted-by":"publisher","first-page":"11545","DOI":"10.1021\/jp040280v","article-title":"Spectroscopic\nstudies of the intermediates in the conversion of 1,4,11,12-tetrahydro-9,10-anthraquinone\nto 9,10-anthraquinone by reaction with oxygen under basic conditions","volume":"108","author":"Mattar","year":"2004","journal-title":"J. Phys. Chem. A"},{"issue":"1\u20132","key":"2026090303525518300_cit53","doi-asserted-by":"publisher","first-page":"152","DOI":"10.1016\/S0009-2614(02)01136-3","article-title":"Accurate\ncomputations of the methyl isotropic hyperfine coupling constants\nin 2-methyl-1,4-benzosemiquinone radical intermediate","volume":"363","author":"Mattar","year":"2002","journal-title":"Chem. Phys. Lett."},{"issue":"1\u20132","key":"2026090303525518300_cit54","doi-asserted-by":"publisher","first-page":"39","DOI":"10.1016\/S0009-2614(01)01415-4","article-title":"Generation\nand spectroscopic characterization of the 2,3,5,6-tetramethoxy-1,4-benzosemiquinone\nreactive intermediate","volume":"352","author":"Mattar","year":"2002","journal-title":"Chem. Phys. Lett."},{"issue":"14","key":"2026090303525518300_cit55","doi-asserted-by":"publisher","first-page":"4194","DOI":"10.1039\/C9AN00468H","article-title":"Embedding cyclic nitrone\nin mesoporous silica particles for EPR spin trapping of superoxide\nand other radicals","volume":"144","author":"Besson","year":"2019","journal-title":"Analyst"},{"issue":"7","key":"2026090303525518300_cit56","doi-asserted-by":"publisher","first-page":"737","DOI":"10.1080\/10715762.2019.1624741","article-title":"Formation of methyl radicals derived\nfrom cumene hydroperoxide in reconstructed human epidermis: an EPR\nspin trapping confirmation by using C-13-substitution","volume":"53","author":"Sahli","year":"2019","journal-title":"Free Radical Res."},{"key":"2026090303525518300_cit57","doi-asserted-by":"publisher","first-page":"1020","DOI":"10.1002\/ijch.201900074","article-title":"A New and Robust Method\nfor In-situ EPR Electrochemistry","volume":"59","author":"Toybenshlak","year":"2019","journal-title":"Isr. J. Chem."},{"issue":"2","key":"2026090303525518300_cit58","doi-asserted-by":"publisher","first-page":"300","DOI":"10.1021\/bi401164k","article-title":"pH dependence of amylin fibrillization","volume":"53","author":"Jha","year":"2014","journal-title":"Biochemistry"},{"key":"2026090303525518300_cit59","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.bpc.2016.09.007","article-title":"Amyloidogenesis\nof the amylin analogue pramlintide","volume":"219","author":"da Silva","year":"2016","journal-title":"Biophys.\nChem."},{"key":"2026090303525518300_cit60","doi-asserted-by":"publisher","first-page":"58","DOI":"10.1016\/j.bpc.2016.09.008","article-title":"Regulation\nof the assembly and amyloid aggregation of murine amylin by zinc","volume":"218","author":"Erthal","year":"2016","journal-title":"Biophys. 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