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      Platinum(II) O, S Complexes Inhibit the Aggregation of Amyloid Model Systems

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          Abstract

          Platinum(II) complexes with different cinnamic acid derivatives as ligands were investigated for their ability to inhibit the aggregation process of amyloid systems derived from Aβ, Yeast Prion Protein Sup35p and the C-terminal domain of nucleophosmin 1. Thioflavin T binding assays and circular dichroism data indicate that these compounds strongly inhibit the aggregation of investigated peptides exhibiting IC 50 values in the micromolar range. MS analysis confirms the formation of adducts between peptides and Pt(II) complexes that are also able to reduce amyloid cytotoxicity in human SH-SY5Y neuroblastoma cells. Overall data suggests that bidentate ligands based on β-hydroxy dithiocinnamic esters can be used to develop platinum or platinoid compounds with anti-amyloid aggregation properties.

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          Crystal structure of double-stranded DNA containing the major adduct of the anticancer drug cisplatin.

          P M Takahara, A C Rosenzweig, C A Frederick … (1995)
          The success of cisplatin in cancer chemotherapy derives from its ability to crosslink DNA and alter the structure. Most cisplatin-DNA adducts are intrastrand d(GpG) and d(ApG) crosslinks, which unwind and bend the duplex to facilitate the binding of proteins that contain one or more high-mobility group (HMG) domains. When HMG-domain proteins such as HMG1, IXR (intrastrand-crosslink recognition) protein from yeast, or human upstream-binding factor (hUBF) bind cisplatin intrastrand crosslinks, they can be diverted from their natural binding sites on the genome and shield the adducts from excision repair. These activities sensitize cells to cisplatin and contribute to its cytotoxic properties. Crystallographic information about the structure of cisplatin-DNA adducts has been limited to short single-stranded deoxyoligonucleotides such as cis-[Pt(NH3)2(d(pGpG))]. Here we describe the X-ray structure at 2.6 A resolution of a double-stranded DNA dodecamer containing this adduct. Our information provides, to our knowledge, the first crystallographic look at a platinated DNA duplex and should help the design of new platinum and other metal crosslinking antitumour drug candidates. Moreover, the structure reveals a unique fusion of A- and B-type DNA segments that could be of more general importance.
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            Metal-associated amyloid-β species in Alzheimer's disease.

            Amit Pithadia, Mi Lim (2012)
            Highly concentrated metals such as Cu, Zn, and Fe are found in amyloid-β (Aβ) plaques within the brain of Alzheimer's disease (AD). In vitro and in vivo studies have suggested that metal binding to Aβ could facilitate Aβ aggregation and generate reactive oxygen species (ROS), which could contribute to the neuropathogenesis of AD. The connection between metal-Aβ interaction/reactivity and AD development, however, has not been clearly revealed owing to the complexity of the disease. In this review, metal-Aβ interaction/reactivity and its relation to neurotoxicity are briefly discussed. Additionally, our review illustrates the recent progress of small molecules, capable of targeting metal-Aβ species and modulating their interaction/reactivity, which could offer a promising approach to interrogate their role in AD. Copyright © 2012 Elsevier Ltd. All rights reserved.
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              An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated beta-sheet structure for amyloid.

              M Balbirnie, R Grothe, D S Eisenberg (2001)
              X-ray diffraction and other biophysical tools reveal features of the atomic structure of an amyloid-like crystal. Sup35, a prion-like protein in yeast, forms fibrillar amyloid assemblies intrinsic to its prion function. We have identified a polar peptide from the N-terminal prion-determining domain of Sup35 that exhibits the amyloid properties of full-length Sup35, including cooperative kinetics of aggregation, fibril formation, binding of the dye Congo red, and the characteristic cross-beta x-ray diffraction pattern. Microcrystals of this peptide also share the principal properties of the fibrillar amyloid, including a highly stable, beta-sheet-rich structure and the binding of Congo red. The x-ray powder pattern of the microcrystals, extending to 0.9-A resolution, yields the unit cell dimensions of the well-ordered structure. These dimensions restrict possible atomic models of this amyloid-like structure and demonstrate that it forms packed, parallel-stranded beta-sheets. The unusually high density of the crystals shows that the packed beta-sheets are dehydrated, despite the polar character of the side chains. These results suggest that amyloid is a highly intermolecularly bonded, dehydrated array of densely packed beta-sheets. This dry beta-sheet could form as Sup35 partially unfolds to expose the peptide, permitting it to hydrogen-bond to the same peptide of other Sup35 molecules. The implication is that amyloid-forming units may be short segments of proteins, exposed for interactions by partial unfolding.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Int J Mol Sci
                Journal ID (iso-abbrev): Int J Mol Sci
                Journal ID (publisher-id): ijms
                Title: International Journal of Molecular Sciences
                Publisher: MDPI
                ISSN (Electronic): 1422-0067
                Publication date (Electronic): 14 February 2019
                Publication date Collection: February 2019
                Volume: 20
                Issue: 4
                Electronic Location Identifier: 829
                Affiliations
                [1 ]Department of Pharmacy, University of Naples Federico II, 80134 Napoli, Italy; floriodaniele1@ 123456gmail.com (D.F.); giancarlo.morelli@ 123456unina.it (G.M.)
                [2 ]Department of Translational Medical Science, University of Naples Federico II, 80131 Napoli, Italy; annamaria.malfitano@ 123456unina.it (A.M.M.); sarah.disomma@ 123456unina.it (S.D.S.)
                [3 ]Institute for Inorganic and Analytical Chemistry, University of Jena, 07743 Jena, Germany; carolin.muegge@ 123456rub.de (C.M.); wolfgang.weigand@ 123456uni-jena.de (W.W.)
                [4 ]Department of Biology, Ruhr-University Bochum, 44801 Bochum, Germany
                [5 ]Department of Chemical Sciences, University of Naples Federico II, 80126 Napoli, Italy; giarita.ferraro@ 123456gmail.com (G.F.); ilaria.iacobucci@ 123456unina.it (I.I.); montimar@ 123456unina.it (M.M.); antonello.merlino@ 123456unina.it (A.M.)
                [6 ]CEINGE Biotecnologie Avanzate s.c.a r.l., University of Naples Federico II, 80145 Napoli, Italy
                Author notes
                [* ]Correspondence: daniela.marasco@ 123456unina.it ; Tel.: +39-0812534607
                Author information
                https://orcid.org/0000-0002-8065-173X
                https://orcid.org/0000-0001-5177-1006
                https://orcid.org/0000-0002-7775-7154
                https://orcid.org/0000-0002-1045-7720
                Article
                Publisher ID: ijms-20-00829
                DOI: 10.3390/ijms20040829
                PMC ID: 6413125
                PubMed ID: 30769904
                SO-VID: a08a3f05-f756-4fef-879c-22b57ae45652
                Copyright © © 2019 by the authors.
                License:

                Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( http://creativecommons.org/licenses/by/4.0/).

                History
                Date received : 11 January 2019
                Date accepted : 13 February 2019
                Categories
                Subject: Article

                ScienceOpen disciplines: Molecular biology
                Keywords: amyloid aggregation,platinum complexes,anti-aggregation properties
                Data availability:
                ScienceOpen disciplines: Molecular biology
                Keywords: amyloid aggregation, platinum complexes, anti-aggregation properties

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