Complexation of Amyloid Fibrils with Charged Conjugated Polymers
It has been suggested that conjugated charged polymers are amyloid imaging agents and promising therapeutic candidates for neurological disorders. However, very less is known about their efficacy in modulating the amyloid aggregation pathway. Here, we studied the modulation of Parkinson’s disease as...
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Veröffentlicht in: | Langmuir 2014-04, Vol.30 (13), p.3775-3786 |
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creator | Ghosh, Dhiman Dutta, Paulami Chakraborty, Chanchal Singh, Pradeep K Anoop, A Jha, Narendra Nath Jacob, Reeba S Mondal, Mrityunjoy Mankar, Shruti Das, Subhadeep Malik, Sudip Maji, Samir K |
description | It has been suggested that conjugated charged polymers are amyloid imaging agents and promising therapeutic candidates for neurological disorders. However, very less is known about their efficacy in modulating the amyloid aggregation pathway. Here, we studied the modulation of Parkinson’s disease associated α-synuclein (AS) amyloid assembly kinetics using conjugated polyfluorene polymers (PF, cationic; PFS, anionic). We also explored the complexation of these charged polymers with the various AS aggregated species including amyloid fibrils and oligomers using multidisciplinary biophysical techniques. Our data suggests that both polymers irrespective of their different charges in the side chains increase the fibrilization kinetics of AS and also remarkably change the morphology of the resultant amyloid fibrils. Both polymers were incorporated/aligned onto the AS amyloid fibrils as evident from electron microscopy (EM) and atomic force microscopy (AFM), and the resultant complexes were structurally distinct from their pristine form of both polymers and AS supported by FTIR study. Additionally, we observed that the mechanism of interactions between the polymers with different species of AS aggregates were markedly different. |
doi_str_mv | 10.1021/la404739f |
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However, very less is known about their efficacy in modulating the amyloid aggregation pathway. Here, we studied the modulation of Parkinson’s disease associated α-synuclein (AS) amyloid assembly kinetics using conjugated polyfluorene polymers (PF, cationic; PFS, anionic). We also explored the complexation of these charged polymers with the various AS aggregated species including amyloid fibrils and oligomers using multidisciplinary biophysical techniques. Our data suggests that both polymers irrespective of their different charges in the side chains increase the fibrilization kinetics of AS and also remarkably change the morphology of the resultant amyloid fibrils. Both polymers were incorporated/aligned onto the AS amyloid fibrils as evident from electron microscopy (EM) and atomic force microscopy (AFM), and the resultant complexes were structurally distinct from their pristine form of both polymers and AS supported by FTIR study. Additionally, we observed that the mechanism of interactions between the polymers with different species of AS aggregates were markedly different.</description><identifier>ISSN: 0743-7463</identifier><identifier>EISSN: 1520-5827</identifier><identifier>DOI: 10.1021/la404739f</identifier><identifier>PMID: 24678792</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>alpha-Synuclein - chemistry ; alpha-Synuclein - genetics ; Amino Acid Sequence ; Amyloid - chemistry ; Escherichia coli - genetics ; Escherichia coli - metabolism ; Fluorocarbon Polymers - chemical synthesis ; Fluorocarbon Polymers - chemistry ; Gene Expression ; Humans ; Kinetics ; Microscopy, Atomic Force ; Molecular Sequence Data ; Protein Aggregates ; Recombinant Proteins - chemistry ; Recombinant Proteins - genetics ; Solutions ; Spectroscopy, Fourier Transform Infrared ; Static Electricity ; Thiazoles</subject><ispartof>Langmuir, 2014-04, Vol.30 (13), p.3775-3786</ispartof><rights>Copyright © 2014 American Chemical Society</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a315t-e82800330d6cf9de830e13e0cc024c458b6e03654acc2332436a9bdcaab568493</citedby><cites>FETCH-LOGICAL-a315t-e82800330d6cf9de830e13e0cc024c458b6e03654acc2332436a9bdcaab568493</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/la404739f$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/la404739f$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,776,780,2752,27053,27901,27902,56713,56763</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24678792$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ghosh, Dhiman</creatorcontrib><creatorcontrib>Dutta, Paulami</creatorcontrib><creatorcontrib>Chakraborty, Chanchal</creatorcontrib><creatorcontrib>Singh, Pradeep K</creatorcontrib><creatorcontrib>Anoop, A</creatorcontrib><creatorcontrib>Jha, Narendra Nath</creatorcontrib><creatorcontrib>Jacob, Reeba S</creatorcontrib><creatorcontrib>Mondal, Mrityunjoy</creatorcontrib><creatorcontrib>Mankar, Shruti</creatorcontrib><creatorcontrib>Das, Subhadeep</creatorcontrib><creatorcontrib>Malik, Sudip</creatorcontrib><creatorcontrib>Maji, Samir K</creatorcontrib><title>Complexation of Amyloid Fibrils with Charged Conjugated Polymers</title><title>Langmuir</title><addtitle>Langmuir</addtitle><description>It has been suggested that conjugated charged polymers are amyloid imaging agents and promising therapeutic candidates for neurological disorders. However, very less is known about their efficacy in modulating the amyloid aggregation pathway. Here, we studied the modulation of Parkinson’s disease associated α-synuclein (AS) amyloid assembly kinetics using conjugated polyfluorene polymers (PF, cationic; PFS, anionic). We also explored the complexation of these charged polymers with the various AS aggregated species including amyloid fibrils and oligomers using multidisciplinary biophysical techniques. Our data suggests that both polymers irrespective of their different charges in the side chains increase the fibrilization kinetics of AS and also remarkably change the morphology of the resultant amyloid fibrils. Both polymers were incorporated/aligned onto the AS amyloid fibrils as evident from electron microscopy (EM) and atomic force microscopy (AFM), and the resultant complexes were structurally distinct from their pristine form of both polymers and AS supported by FTIR study. Additionally, we observed that the mechanism of interactions between the polymers with different species of AS aggregates were markedly different.</description><subject>alpha-Synuclein - chemistry</subject><subject>alpha-Synuclein - genetics</subject><subject>Amino Acid Sequence</subject><subject>Amyloid - chemistry</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli - metabolism</subject><subject>Fluorocarbon Polymers - chemical synthesis</subject><subject>Fluorocarbon Polymers - chemistry</subject><subject>Gene Expression</subject><subject>Humans</subject><subject>Kinetics</subject><subject>Microscopy, Atomic Force</subject><subject>Molecular Sequence Data</subject><subject>Protein Aggregates</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - genetics</subject><subject>Solutions</subject><subject>Spectroscopy, Fourier Transform Infrared</subject><subject>Static Electricity</subject><subject>Thiazoles</subject><issn>0743-7463</issn><issn>1520-5827</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkDFPwzAQRi0EoqUw8AdQFiQYAmefkzgbVUQBqRIMMEeO47SpnLjYiSD_nqCWTkx3w9OTvkfIJYU7CozeG8mBJ5hWR2RKIwZhJFhyTKaQcAwTHuOEnHm_AYAUeXpKJozHiUhSNiUPmW22Rn_LrrZtYKtg3gzG1mWwqAtXGx981d06yNbSrXQZZLbd9CvZje-bNUOjnT8nJ5U0Xl_s74x8LB7fs-dw-fr0ks2XoUQadaEWTAAgQhmrKi21QNAUNSgFjCseiSLWgHHEpVIMkXGMZVqUSsoiigVPcUZudt6ts5-99l3e1F5pY2Srbe9zGlHOcRwsRvR2hypnvXe6yreubqQbcgr5b7D8EGxkr_bavmh0eSD_Co3A9Q6Qyucb27t2XPmP6AfmGHCz</recordid><startdate>20140408</startdate><enddate>20140408</enddate><creator>Ghosh, Dhiman</creator><creator>Dutta, Paulami</creator><creator>Chakraborty, Chanchal</creator><creator>Singh, Pradeep K</creator><creator>Anoop, A</creator><creator>Jha, Narendra Nath</creator><creator>Jacob, Reeba S</creator><creator>Mondal, Mrityunjoy</creator><creator>Mankar, Shruti</creator><creator>Das, Subhadeep</creator><creator>Malik, Sudip</creator><creator>Maji, Samir K</creator><general>American Chemical Society</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>7X8</scope></search><sort><creationdate>20140408</creationdate><title>Complexation of Amyloid Fibrils with Charged Conjugated Polymers</title><author>Ghosh, Dhiman ; Dutta, Paulami ; Chakraborty, Chanchal ; Singh, Pradeep K ; Anoop, A ; Jha, Narendra Nath ; Jacob, Reeba S ; Mondal, Mrityunjoy ; Mankar, Shruti ; Das, Subhadeep ; Malik, Sudip ; Maji, Samir K</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a315t-e82800330d6cf9de830e13e0cc024c458b6e03654acc2332436a9bdcaab568493</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>alpha-Synuclein - chemistry</topic><topic>alpha-Synuclein - genetics</topic><topic>Amino Acid Sequence</topic><topic>Amyloid - chemistry</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli - metabolism</topic><topic>Fluorocarbon Polymers - chemical synthesis</topic><topic>Fluorocarbon Polymers - chemistry</topic><topic>Gene Expression</topic><topic>Humans</topic><topic>Kinetics</topic><topic>Microscopy, Atomic Force</topic><topic>Molecular Sequence Data</topic><topic>Protein Aggregates</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - genetics</topic><topic>Solutions</topic><topic>Spectroscopy, Fourier Transform Infrared</topic><topic>Static Electricity</topic><topic>Thiazoles</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ghosh, Dhiman</creatorcontrib><creatorcontrib>Dutta, Paulami</creatorcontrib><creatorcontrib>Chakraborty, Chanchal</creatorcontrib><creatorcontrib>Singh, Pradeep K</creatorcontrib><creatorcontrib>Anoop, A</creatorcontrib><creatorcontrib>Jha, Narendra Nath</creatorcontrib><creatorcontrib>Jacob, Reeba S</creatorcontrib><creatorcontrib>Mondal, Mrityunjoy</creatorcontrib><creatorcontrib>Mankar, Shruti</creatorcontrib><creatorcontrib>Das, Subhadeep</creatorcontrib><creatorcontrib>Malik, Sudip</creatorcontrib><creatorcontrib>Maji, Samir K</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Langmuir</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ghosh, Dhiman</au><au>Dutta, Paulami</au><au>Chakraborty, Chanchal</au><au>Singh, Pradeep K</au><au>Anoop, A</au><au>Jha, Narendra Nath</au><au>Jacob, Reeba S</au><au>Mondal, Mrityunjoy</au><au>Mankar, Shruti</au><au>Das, Subhadeep</au><au>Malik, Sudip</au><au>Maji, Samir K</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Complexation of Amyloid Fibrils with Charged Conjugated Polymers</atitle><jtitle>Langmuir</jtitle><addtitle>Langmuir</addtitle><date>2014-04-08</date><risdate>2014</risdate><volume>30</volume><issue>13</issue><spage>3775</spage><epage>3786</epage><pages>3775-3786</pages><issn>0743-7463</issn><eissn>1520-5827</eissn><abstract>It has been suggested that conjugated charged polymers are amyloid imaging agents and promising therapeutic candidates for neurological disorders. However, very less is known about their efficacy in modulating the amyloid aggregation pathway. Here, we studied the modulation of Parkinson’s disease associated α-synuclein (AS) amyloid assembly kinetics using conjugated polyfluorene polymers (PF, cationic; PFS, anionic). We also explored the complexation of these charged polymers with the various AS aggregated species including amyloid fibrils and oligomers using multidisciplinary biophysical techniques. Our data suggests that both polymers irrespective of their different charges in the side chains increase the fibrilization kinetics of AS and also remarkably change the morphology of the resultant amyloid fibrils. Both polymers were incorporated/aligned onto the AS amyloid fibrils as evident from electron microscopy (EM) and atomic force microscopy (AFM), and the resultant complexes were structurally distinct from their pristine form of both polymers and AS supported by FTIR study. 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subjects | alpha-Synuclein - chemistry alpha-Synuclein - genetics Amino Acid Sequence Amyloid - chemistry Escherichia coli - genetics Escherichia coli - metabolism Fluorocarbon Polymers - chemical synthesis Fluorocarbon Polymers - chemistry Gene Expression Humans Kinetics Microscopy, Atomic Force Molecular Sequence Data Protein Aggregates Recombinant Proteins - chemistry Recombinant Proteins - genetics Solutions Spectroscopy, Fourier Transform Infrared Static Electricity Thiazoles |
title | Complexation of Amyloid Fibrils with Charged Conjugated Polymers |
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