A Comparative Study of the Effects of Platinum (II) Complexes on β-Amyloid Aggregation: Potential Neurodrug Applications
Herein the effects of three platinum complexes, namely ( -4-2)-(2,2'-bipyridine)dichloridoplatinum(II), Pt-bpy, ( -4-2)-dichlorido(1,10-phenanthroline) platinum(II), Pt-phen, and ( -4-2)-chlorido(2,2':6',2''-terpyridine)platinum(II) chloride, Pt-terpy, on the aggregation of...
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creator | Manna, Sara La Florio, Daniele Iacobucci, Ilaria Napolitano, Fabiana Benedictis, Ilaria De Malfitano, Anna Maria Monti, Maria Ravera, Mauro Gabano, Elisabetta Marasco, Daniela |
description | Herein the effects of three platinum complexes, namely (
-4-2)-(2,2'-bipyridine)dichloridoplatinum(II), Pt-bpy, (
-4-2)-dichlorido(1,10-phenanthroline) platinum(II), Pt-phen, and (
-4-2)-chlorido(2,2':6',2''-terpyridine)platinum(II) chloride, Pt-terpy, on the aggregation of an amyloid model system derived from the C-terminal domain of Aβ peptide (Aβ
) were investigated. Thioflavin T (ThT) binding assays revealed the ability of Pt(II) compounds to repress amyloid aggregation in a dose-dependent way, whereas the ability of Aβ
peptide to interfere with ligand field of metal complexes was analyzed through UV-Vis absorption spectroscopy and electrospray ionization mass spectrometry. Spectroscopic data provided micromolar EC
values and allowed to assess that the observed inhibition of amyloid aggregation is due to the formation of adducts between Aβ
peptide and complexes upon the release of labile ligands as chloride and that they can explore different modes of coordination toward Aβ
with respect to the entire Aβ
polypeptide. In addition, conformational studies through circular dichroism (CD) spectroscopy suggested that Pt-terpy induces soluble β-structures of monomeric Aβ
, thus limiting self-recognition. Noticeably, Pt-terpy demonstrated the ability to reduce the cytotoxicity of amyloid peptide in human SH-SY5Y neuroblastoma cells. Presented data corroborate the hypothesis to enlarge the application field of already known metal-based agents to neurodegenerative diseases, as potential neurodrugs. |
doi_str_mv | 10.3390/ijms22063015 |
format | Article |
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-4-2)-(2,2'-bipyridine)dichloridoplatinum(II), Pt-bpy, (
-4-2)-dichlorido(1,10-phenanthroline) platinum(II), Pt-phen, and (
-4-2)-chlorido(2,2':6',2''-terpyridine)platinum(II) chloride, Pt-terpy, on the aggregation of an amyloid model system derived from the C-terminal domain of Aβ peptide (Aβ
) were investigated. Thioflavin T (ThT) binding assays revealed the ability of Pt(II) compounds to repress amyloid aggregation in a dose-dependent way, whereas the ability of Aβ
peptide to interfere with ligand field of metal complexes was analyzed through UV-Vis absorption spectroscopy and electrospray ionization mass spectrometry. Spectroscopic data provided micromolar EC
values and allowed to assess that the observed inhibition of amyloid aggregation is due to the formation of adducts between Aβ
peptide and complexes upon the release of labile ligands as chloride and that they can explore different modes of coordination toward Aβ
with respect to the entire Aβ
polypeptide. In addition, conformational studies through circular dichroism (CD) spectroscopy suggested that Pt-terpy induces soluble β-structures of monomeric Aβ
, thus limiting self-recognition. Noticeably, Pt-terpy demonstrated the ability to reduce the cytotoxicity of amyloid peptide in human SH-SY5Y neuroblastoma cells. Presented data corroborate the hypothesis to enlarge the application field of already known metal-based agents to neurodegenerative diseases, as potential neurodrugs.</description><identifier>ISSN: 1422-0067</identifier><identifier>ISSN: 1661-6596</identifier><identifier>EISSN: 1422-0067</identifier><identifier>DOI: 10.3390/ijms22063015</identifier><identifier>PMID: 33809522</identifier><language>eng</language><publisher>Switzerland: MDPI AG</publisher><subject>Absorption spectroscopy ; Adducts ; Alzheimer's disease ; Amino Acid Sequence ; Amyloid beta-Peptides - chemistry ; Benzothiazoles - metabolism ; Cell Death - drug effects ; Cell Line, Tumor ; Cell Proliferation - drug effects ; Chloride ; Chlorides ; Circular dichroism ; Comparative studies ; Cytotoxicity ; Dichroism ; Fluorescence ; Humans ; Investigations ; Ligands ; Mass spectrometry ; Mass spectroscopy ; Neuroblasts ; Peptide Fragments - chemistry ; Peptides ; Platinum ; Platinum - chemistry ; Platinum - pharmacology ; Polypeptides ; Protein Aggregates - drug effects ; Protein Stability ; Scientific imaging ; Self-recognition ; Solubility ; Spectrophotometry, Ultraviolet ; Time Factors ; β-Amyloid</subject><ispartof>International journal of molecular sciences, 2021-03, Vol.22 (6), p.3015</ispartof><rights>2021. This work is licensed under http://creativecommons.org/licenses/by/3.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2021 by the authors. 2021</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c412t-9afde22c2b6517758c7a972c8f18d57c807f65023b20164c9f04d9a0ee04aa83</citedby><cites>FETCH-LOGICAL-c412t-9afde22c2b6517758c7a972c8f18d57c807f65023b20164c9f04d9a0ee04aa83</cites><orcidid>0000-0002-4732-7508 ; 0000-0002-1181-1955 ; 0000-0001-7762-0708 ; 0000-0002-9242-6046 ; 0000-0002-7775-7154 ; 0000-0001-6210-5607 ; 0000-0002-6193-2835 ; 0000-0002-6618-2949</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7998721/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7998721/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/33809522$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Manna, Sara La</creatorcontrib><creatorcontrib>Florio, Daniele</creatorcontrib><creatorcontrib>Iacobucci, Ilaria</creatorcontrib><creatorcontrib>Napolitano, Fabiana</creatorcontrib><creatorcontrib>Benedictis, Ilaria De</creatorcontrib><creatorcontrib>Malfitano, Anna Maria</creatorcontrib><creatorcontrib>Monti, Maria</creatorcontrib><creatorcontrib>Ravera, Mauro</creatorcontrib><creatorcontrib>Gabano, Elisabetta</creatorcontrib><creatorcontrib>Marasco, Daniela</creatorcontrib><title>A Comparative Study of the Effects of Platinum (II) Complexes on β-Amyloid Aggregation: Potential Neurodrug Applications</title><title>International journal of molecular sciences</title><addtitle>Int J Mol Sci</addtitle><description>Herein the effects of three platinum complexes, namely (
-4-2)-(2,2'-bipyridine)dichloridoplatinum(II), Pt-bpy, (
-4-2)-dichlorido(1,10-phenanthroline) platinum(II), Pt-phen, and (
-4-2)-chlorido(2,2':6',2''-terpyridine)platinum(II) chloride, Pt-terpy, on the aggregation of an amyloid model system derived from the C-terminal domain of Aβ peptide (Aβ
) were investigated. Thioflavin T (ThT) binding assays revealed the ability of Pt(II) compounds to repress amyloid aggregation in a dose-dependent way, whereas the ability of Aβ
peptide to interfere with ligand field of metal complexes was analyzed through UV-Vis absorption spectroscopy and electrospray ionization mass spectrometry. Spectroscopic data provided micromolar EC
values and allowed to assess that the observed inhibition of amyloid aggregation is due to the formation of adducts between Aβ
peptide and complexes upon the release of labile ligands as chloride and that they can explore different modes of coordination toward Aβ
with respect to the entire Aβ
polypeptide. In addition, conformational studies through circular dichroism (CD) spectroscopy suggested that Pt-terpy induces soluble β-structures of monomeric Aβ
, thus limiting self-recognition. Noticeably, Pt-terpy demonstrated the ability to reduce the cytotoxicity of amyloid peptide in human SH-SY5Y neuroblastoma cells. Presented data corroborate the hypothesis to enlarge the application field of already known metal-based agents to neurodegenerative diseases, as potential neurodrugs.</description><subject>Absorption spectroscopy</subject><subject>Adducts</subject><subject>Alzheimer's disease</subject><subject>Amino Acid Sequence</subject><subject>Amyloid beta-Peptides - chemistry</subject><subject>Benzothiazoles - metabolism</subject><subject>Cell Death - drug effects</subject><subject>Cell Line, Tumor</subject><subject>Cell Proliferation - drug effects</subject><subject>Chloride</subject><subject>Chlorides</subject><subject>Circular dichroism</subject><subject>Comparative studies</subject><subject>Cytotoxicity</subject><subject>Dichroism</subject><subject>Fluorescence</subject><subject>Humans</subject><subject>Investigations</subject><subject>Ligands</subject><subject>Mass spectrometry</subject><subject>Mass spectroscopy</subject><subject>Neuroblasts</subject><subject>Peptide Fragments - chemistry</subject><subject>Peptides</subject><subject>Platinum</subject><subject>Platinum - chemistry</subject><subject>Platinum - pharmacology</subject><subject>Polypeptides</subject><subject>Protein Aggregates - drug effects</subject><subject>Protein Stability</subject><subject>Scientific imaging</subject><subject>Self-recognition</subject><subject>Solubility</subject><subject>Spectrophotometry, Ultraviolet</subject><subject>Time Factors</subject><subject>β-Amyloid</subject><issn>1422-0067</issn><issn>1661-6596</issn><issn>1422-0067</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNpdkV1rFDEYhYMo9kPvvJaANy04mo_JJPFCGJaqC0UL9j5kM8k0S2YyJjPF_Vv-EH-T2baW1au84Tzv4T0cAF5h9I5Sid777ZAJQQ1FmD0Bx7gmpEKo4U8P5iNwkvMWIUIJk8_BEaUCSUbIMdi1cBWHSSc9-1sLv89Lt4PRwfnGwgvnrJnz_nsVij4uAzxbr8_vNoL9aYs0wt-_qnbYheg72PZ9sn0h4_gBXsXZjrPXAX61S4pdWnrYTlPw5g7IL8Azp0O2Lx_eU3D96eJ69aW6_PZ5vWovK1NjMldSu84SYsimYZhzJgzXkhMjHBYd40Yg7hpWkm0Iwk1tpEN1JzWyFtVaC3oKPt7bTstmsJ0pNyUd1JT8oNNORe3Vv8rob1QfbxWXUnCCi8HZg0GKPxabZzX4bGwIerRxyYowJFiBCSnom__QbVzSWNLtKUqZ4HJPvb2nTIo5J-sej8FI7StVh5UW_PVhgEf4b4f0D1oeniQ</recordid><startdate>20210316</startdate><enddate>20210316</enddate><creator>Manna, Sara La</creator><creator>Florio, Daniele</creator><creator>Iacobucci, Ilaria</creator><creator>Napolitano, Fabiana</creator><creator>Benedictis, Ilaria De</creator><creator>Malfitano, Anna Maria</creator><creator>Monti, Maria</creator><creator>Ravera, Mauro</creator><creator>Gabano, Elisabetta</creator><creator>Marasco, Daniela</creator><general>MDPI AG</general><general>MDPI</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>K9.</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>MBDVC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-4732-7508</orcidid><orcidid>https://orcid.org/0000-0002-1181-1955</orcidid><orcidid>https://orcid.org/0000-0001-7762-0708</orcidid><orcidid>https://orcid.org/0000-0002-9242-6046</orcidid><orcidid>https://orcid.org/0000-0002-7775-7154</orcidid><orcidid>https://orcid.org/0000-0001-6210-5607</orcidid><orcidid>https://orcid.org/0000-0002-6193-2835</orcidid><orcidid>https://orcid.org/0000-0002-6618-2949</orcidid></search><sort><creationdate>20210316</creationdate><title>A Comparative Study of the Effects of Platinum (II) Complexes on β-Amyloid Aggregation: Potential Neurodrug Applications</title><author>Manna, Sara La ; Florio, Daniele ; Iacobucci, Ilaria ; Napolitano, Fabiana ; Benedictis, Ilaria De ; Malfitano, Anna Maria ; Monti, Maria ; Ravera, Mauro ; Gabano, Elisabetta ; Marasco, Daniela</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c412t-9afde22c2b6517758c7a972c8f18d57c807f65023b20164c9f04d9a0ee04aa83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>Absorption spectroscopy</topic><topic>Adducts</topic><topic>Alzheimer's disease</topic><topic>Amino Acid Sequence</topic><topic>Amyloid beta-Peptides - chemistry</topic><topic>Benzothiazoles - metabolism</topic><topic>Cell Death - drug effects</topic><topic>Cell Line, Tumor</topic><topic>Cell Proliferation - drug effects</topic><topic>Chloride</topic><topic>Chlorides</topic><topic>Circular dichroism</topic><topic>Comparative studies</topic><topic>Cytotoxicity</topic><topic>Dichroism</topic><topic>Fluorescence</topic><topic>Humans</topic><topic>Investigations</topic><topic>Ligands</topic><topic>Mass spectrometry</topic><topic>Mass spectroscopy</topic><topic>Neuroblasts</topic><topic>Peptide Fragments - chemistry</topic><topic>Peptides</topic><topic>Platinum</topic><topic>Platinum - chemistry</topic><topic>Platinum - pharmacology</topic><topic>Polypeptides</topic><topic>Protein Aggregates - drug effects</topic><topic>Protein Stability</topic><topic>Scientific imaging</topic><topic>Self-recognition</topic><topic>Solubility</topic><topic>Spectrophotometry, Ultraviolet</topic><topic>Time Factors</topic><topic>β-Amyloid</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Manna, Sara La</creatorcontrib><creatorcontrib>Florio, Daniele</creatorcontrib><creatorcontrib>Iacobucci, Ilaria</creatorcontrib><creatorcontrib>Napolitano, Fabiana</creatorcontrib><creatorcontrib>Benedictis, Ilaria De</creatorcontrib><creatorcontrib>Malfitano, Anna Maria</creatorcontrib><creatorcontrib>Monti, Maria</creatorcontrib><creatorcontrib>Ravera, Mauro</creatorcontrib><creatorcontrib>Gabano, Elisabetta</creatorcontrib><creatorcontrib>Marasco, Daniela</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Research Library (Corporate)</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>International journal of molecular sciences</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Manna, Sara La</au><au>Florio, Daniele</au><au>Iacobucci, Ilaria</au><au>Napolitano, Fabiana</au><au>Benedictis, Ilaria De</au><au>Malfitano, Anna Maria</au><au>Monti, Maria</au><au>Ravera, Mauro</au><au>Gabano, Elisabetta</au><au>Marasco, Daniela</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A Comparative Study of the Effects of Platinum (II) Complexes on β-Amyloid Aggregation: Potential Neurodrug Applications</atitle><jtitle>International journal of molecular sciences</jtitle><addtitle>Int J Mol Sci</addtitle><date>2021-03-16</date><risdate>2021</risdate><volume>22</volume><issue>6</issue><spage>3015</spage><pages>3015-</pages><issn>1422-0067</issn><issn>1661-6596</issn><eissn>1422-0067</eissn><abstract>Herein the effects of three platinum complexes, namely (
-4-2)-(2,2'-bipyridine)dichloridoplatinum(II), Pt-bpy, (
-4-2)-dichlorido(1,10-phenanthroline) platinum(II), Pt-phen, and (
-4-2)-chlorido(2,2':6',2''-terpyridine)platinum(II) chloride, Pt-terpy, on the aggregation of an amyloid model system derived from the C-terminal domain of Aβ peptide (Aβ
) were investigated. Thioflavin T (ThT) binding assays revealed the ability of Pt(II) compounds to repress amyloid aggregation in a dose-dependent way, whereas the ability of Aβ
peptide to interfere with ligand field of metal complexes was analyzed through UV-Vis absorption spectroscopy and electrospray ionization mass spectrometry. Spectroscopic data provided micromolar EC
values and allowed to assess that the observed inhibition of amyloid aggregation is due to the formation of adducts between Aβ
peptide and complexes upon the release of labile ligands as chloride and that they can explore different modes of coordination toward Aβ
with respect to the entire Aβ
polypeptide. In addition, conformational studies through circular dichroism (CD) spectroscopy suggested that Pt-terpy induces soluble β-structures of monomeric Aβ
, thus limiting self-recognition. Noticeably, Pt-terpy demonstrated the ability to reduce the cytotoxicity of amyloid peptide in human SH-SY5Y neuroblastoma cells. Presented data corroborate the hypothesis to enlarge the application field of already known metal-based agents to neurodegenerative diseases, as potential neurodrugs.</abstract><cop>Switzerland</cop><pub>MDPI AG</pub><pmid>33809522</pmid><doi>10.3390/ijms22063015</doi><orcidid>https://orcid.org/0000-0002-4732-7508</orcidid><orcidid>https://orcid.org/0000-0002-1181-1955</orcidid><orcidid>https://orcid.org/0000-0001-7762-0708</orcidid><orcidid>https://orcid.org/0000-0002-9242-6046</orcidid><orcidid>https://orcid.org/0000-0002-7775-7154</orcidid><orcidid>https://orcid.org/0000-0001-6210-5607</orcidid><orcidid>https://orcid.org/0000-0002-6193-2835</orcidid><orcidid>https://orcid.org/0000-0002-6618-2949</orcidid><oa>free_for_read</oa></addata></record> |
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source | MDPI - Multidisciplinary Digital Publishing Institute; MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central |
subjects | Absorption spectroscopy Adducts Alzheimer's disease Amino Acid Sequence Amyloid beta-Peptides - chemistry Benzothiazoles - metabolism Cell Death - drug effects Cell Line, Tumor Cell Proliferation - drug effects Chloride Chlorides Circular dichroism Comparative studies Cytotoxicity Dichroism Fluorescence Humans Investigations Ligands Mass spectrometry Mass spectroscopy Neuroblasts Peptide Fragments - chemistry Peptides Platinum Platinum - chemistry Platinum - pharmacology Polypeptides Protein Aggregates - drug effects Protein Stability Scientific imaging Self-recognition Solubility Spectrophotometry, Ultraviolet Time Factors β-Amyloid |
title | A Comparative Study of the Effects of Platinum (II) Complexes on β-Amyloid Aggregation: Potential Neurodrug Applications |
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