NDLI: New Insight in Copper-Ion Binding to Human Islet Amyloid: The Contribution of Metal-Complex Speciation To Reveal the Polypeptide Toxicity

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New Insight in Copper-Ion Binding to Human Islet Amyloid: The Contribution of Metal-Complex Speciation To Reveal the Polypeptide Toxicity

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Magrì, Antonio Nicoletti, Vincenzo Giuseppe Pappalardo, Giuseppe Rizzarelli, Enrico La Mendola, Diego
Description	Author Affiliation: Magrì A ( Consiglio Nazionale delle Ricerche, Istituto di Biostrutture e Bioimmagini, Via P. Gaifami 18, 95126, Catania, Italy. leotony@unict.it.); La Mendola D ( Dipartimento di Farmacia, Università di Pisa, Via Bonanno Pisano, 6, 56126, Pisa, Italy. lamendola@farm.unipi.it.); Nicoletti VG ( Dipartimento di Scienze Biomediche e Biotecnologiche, Università degli Studi di Catania, Viale A. Doria 6, 95125, Catania, Italy.); Pappalardo G ( Consiglio Nazionale delle Ricerche, Istituto di Biostrutture e Bioimmagini, Via P. Gaifami 18, 95126, Catania, Italy.); Rizzarelli E ( Consiglio Nazionale delle Ricerche, Istituto di Biostrutture e Bioimmagini, Via P. Gaifami 18, 95126, Catania, Italy.)
Abstract	Type-2 diabetes (T2D) is considered to be a potential threat on a global level. Recently, T2D has been listed as a misfolding disease, such as Alzheimer's and Parkinson's diseases. Human islet amyloid polypeptide (hIAPP) is a molecule cosecreted in pancreatic β cells and represents the main constituent of an aggregated amyloid found in individuals affected by T2D. The trace-element serum level is significantly influenced during the development of diabetes. In particular, the dys-homeostasis of $Cu^{2+}$ ions may adversely affect the course of the disease. Conflicting results have been reported on the protective role played by complex species formed by $Cu^{2+}$ ions with hIAPP or its peptide fragments in vitro. The histidine (His) residue at position 18 represents the main binding site for the metal ion, but contrasting results have been reported on other residues involved in metal-ion coordination, in particular those toward the N or C terminus. Sequences that encompass regions 17–29 and 14–22 were used to discriminate between the two models of the hIAPP coordination mode. Due to poor solubility in water, poly(ethylene glycol) (PEG) derivatives were synthesized. A peptide fragment that encompasses the 17–29 region of rat amylin (rIAPP) in which the arginine residue at position 18 was substituted by a histidine residue was also obtained to assess that the PEG moiety does not alter the peptide secondary structure. The complex species formed by $Cu^{2+}$ ions with $Ac-PEG-hIAPP(17–29)-NH_{2},$ $Ac-rIAPP(17–29)R18H-NH_{2},$ and $Ac-PEG-hIAPP(14–22)-NH_{2}$ were studied by using potentiometric titrations coupled with spectroscopic methods (UV/Vis, circular dichroism, and EPR). The combined thermodynamic and spectroscopic approach allowed us to demonstrate that hIAPP is able to bind $Cu^{2+}$ ions starting from the His18 imidazole nitrogen atom toward the N-terminus domain. The stability constants of copper(II) complexes with $Ac-PEG-hIAPP(14–22)-NH_{2}$ were used to simulate the different experimental conditions under which aggregate formation and oxidative stress of hIAPP has been reported. Speciation unveils: 1) the protective role played by increased amounts of $Cu^{2+}$ ions on the hIAPP fibrillary aggregation, 2) the effect of adventitious trace amounts of $Cu^{2+}$ ions present in phosphate-buffered saline (PBS), and 3) a reducing fluorogenic probe on $H_{2}O_{2}$ production attributed to the polypeptide alone.
ISSN	09476539
e-ISSN	15213765
Journal	Chemistry - A European Journal
Issue Number	37
Volume Number	22
Language	English
Publisher	Wiley-VCH;ChemPubSoc Europe
Publisher Date	2016-09-05
Publisher Place	Germany
Access Restriction	Open
Subject Keyword	Chemistry
Content Type	Text
Resource Type	Article
Subject	Organic Chemistry Catalysis

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