Does deamidation affect inhibitory mechanisms towards amyloid protein aggregation?
Deamidated amyloid proteins have been shown to accelerate fibril formation. Herein, the results show the inhibition performance and the interaction site between site-specific inhibitor and amyloid protein are significantly influenced by deamidation; while the inhibition mechanism of non-site specifi...
Gespeichert in:
Veröffentlicht in: | Chemical communications (Cambridge, England) England), 2020-08, Vol.56 (68), p.9787-979 |
---|---|
Hauptverfasser: | , , , , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 979 |
---|---|
container_issue | 68 |
container_start_page | 9787 |
container_title | Chemical communications (Cambridge, England) |
container_volume | 56 |
creator | Lam, Yuko P. Y Chiu, Cookson K. C Wootton, Christopher A Hands-Portman, Ian Li, Meng Barrow, Mark P O'Connor, Peter B |
description | Deamidated amyloid proteins have been shown to accelerate fibril formation. Herein, the results show the inhibition performance and the interaction site between site-specific inhibitor and amyloid protein are significantly influenced by deamidation; while the inhibition mechanism of non-site specific inhibitor shows no significant disruption caused by amyloid protein deamidation.
A diagram to show the differences between wild-type and deamidated hIAPPs interaction with site specific and non-specific inhibitors. |
doi_str_mv | 10.1039/d0cc03548c |
format | Article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_crossref_primary_10_1039_D0CC03548C</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2430372232</sourcerecordid><originalsourceid>FETCH-LOGICAL-c399t-f0bfd7cf6d274610071f1ba3e85c6077cf9763986de8791a92d53a8f7da23aa93</originalsourceid><addsrcrecordid>eNp90UlLxDAUB_AgijMuF-9KxYsI1aRpm-Qk0nGDAUEUvJU0y0yGthmTFplvb2ZxBA_mkgfvl8fjHwBOELxGELMbCYWAOEup2AFDhPM0DvXH7rLOWExwmg3AgfczGA7K6D4Y4ISklCE8BK8jq3wkFW-M5J2xbcS1VqKLTDs1lemsW0SNElPeGt_4qLNf3Ekf8WZRWyOjubOdMuHRZOLUZDXg9gjsaV57dby5D8H7w_1b8RSPXx6fi7txLDBjXaxhpSUROpdhmRxBSJBGFceKZiKHJHQYyTGjuVSUMMRZIjPMqSaSJ5hzhg_B5XpuWOKzV74rG-OFqmveKtv7MkkxxCRJcBLoxR86s71rw3ZLldM8pSQL6mqthLPeO6XLuTMNd4sSwXKZdDmCRbFKugj4bDOyrxolt_Qn2gDO18B5se3-flU5lzqY0_8M_gZRdY4g</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2436864875</pqid></control><display><type>article</type><title>Does deamidation affect inhibitory mechanisms towards amyloid protein aggregation?</title><source>MEDLINE</source><source>Royal Society Of Chemistry Journals 2008-</source><source>Alma/SFX Local Collection</source><creator>Lam, Yuko P. Y ; Chiu, Cookson K. C ; Wootton, Christopher A ; Hands-Portman, Ian ; Li, Meng ; Barrow, Mark P ; O'Connor, Peter B</creator><creatorcontrib>Lam, Yuko P. Y ; Chiu, Cookson K. C ; Wootton, Christopher A ; Hands-Portman, Ian ; Li, Meng ; Barrow, Mark P ; O'Connor, Peter B</creatorcontrib><description>Deamidated amyloid proteins have been shown to accelerate fibril formation. Herein, the results show the inhibition performance and the interaction site between site-specific inhibitor and amyloid protein are significantly influenced by deamidation; while the inhibition mechanism of non-site specific inhibitor shows no significant disruption caused by amyloid protein deamidation.
A diagram to show the differences between wild-type and deamidated hIAPPs interaction with site specific and non-specific inhibitors.</description><identifier>ISSN: 1359-7345</identifier><identifier>EISSN: 1364-548X</identifier><identifier>DOI: 10.1039/d0cc03548c</identifier><identifier>PMID: 32748913</identifier><language>eng</language><publisher>England: Royal Society of Chemistry</publisher><subject>Amino Acid Sequence ; Amyloid - chemistry ; Amyloid - metabolism ; Catechin - analogs & derivatives ; Catechin - chemistry ; Catechin - metabolism ; Catechin - pharmacology ; Humans ; Inhibitors ; Islet Amyloid Polypeptide - chemistry ; Islet Amyloid Polypeptide - metabolism ; Microscopy, Electron, Transmission ; Protein Aggregates - drug effects ; Proteins ; Spectrometry, Fluorescence</subject><ispartof>Chemical communications (Cambridge, England), 2020-08, Vol.56 (68), p.9787-979</ispartof><rights>Copyright Royal Society of Chemistry 2020</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c399t-f0bfd7cf6d274610071f1ba3e85c6077cf9763986de8791a92d53a8f7da23aa93</citedby><cites>FETCH-LOGICAL-c399t-f0bfd7cf6d274610071f1ba3e85c6077cf9763986de8791a92d53a8f7da23aa93</cites><orcidid>0000-0002-6588-6274 ; 0000-0001-6967-7675 ; 0000-0002-6944-7009 ; 0000-0002-8895-2342 ; 0000-0002-6474-5357 ; 0000-0002-3647-2611 ; 0000-0001-5486-091X</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/32748913$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lam, Yuko P. Y</creatorcontrib><creatorcontrib>Chiu, Cookson K. C</creatorcontrib><creatorcontrib>Wootton, Christopher A</creatorcontrib><creatorcontrib>Hands-Portman, Ian</creatorcontrib><creatorcontrib>Li, Meng</creatorcontrib><creatorcontrib>Barrow, Mark P</creatorcontrib><creatorcontrib>O'Connor, Peter B</creatorcontrib><title>Does deamidation affect inhibitory mechanisms towards amyloid protein aggregation?</title><title>Chemical communications (Cambridge, England)</title><addtitle>Chem Commun (Camb)</addtitle><description>Deamidated amyloid proteins have been shown to accelerate fibril formation. Herein, the results show the inhibition performance and the interaction site between site-specific inhibitor and amyloid protein are significantly influenced by deamidation; while the inhibition mechanism of non-site specific inhibitor shows no significant disruption caused by amyloid protein deamidation.
A diagram to show the differences between wild-type and deamidated hIAPPs interaction with site specific and non-specific inhibitors.</description><subject>Amino Acid Sequence</subject><subject>Amyloid - chemistry</subject><subject>Amyloid - metabolism</subject><subject>Catechin - analogs & derivatives</subject><subject>Catechin - chemistry</subject><subject>Catechin - metabolism</subject><subject>Catechin - pharmacology</subject><subject>Humans</subject><subject>Inhibitors</subject><subject>Islet Amyloid Polypeptide - chemistry</subject><subject>Islet Amyloid Polypeptide - metabolism</subject><subject>Microscopy, Electron, Transmission</subject><subject>Protein Aggregates - drug effects</subject><subject>Proteins</subject><subject>Spectrometry, Fluorescence</subject><issn>1359-7345</issn><issn>1364-548X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp90UlLxDAUB_AgijMuF-9KxYsI1aRpm-Qk0nGDAUEUvJU0y0yGthmTFplvb2ZxBA_mkgfvl8fjHwBOELxGELMbCYWAOEup2AFDhPM0DvXH7rLOWExwmg3AgfczGA7K6D4Y4ISklCE8BK8jq3wkFW-M5J2xbcS1VqKLTDs1lemsW0SNElPeGt_4qLNf3Ekf8WZRWyOjubOdMuHRZOLUZDXg9gjsaV57dby5D8H7w_1b8RSPXx6fi7txLDBjXaxhpSUROpdhmRxBSJBGFceKZiKHJHQYyTGjuVSUMMRZIjPMqSaSJ5hzhg_B5XpuWOKzV74rG-OFqmveKtv7MkkxxCRJcBLoxR86s71rw3ZLldM8pSQL6mqthLPeO6XLuTMNd4sSwXKZdDmCRbFKugj4bDOyrxolt_Qn2gDO18B5se3-flU5lzqY0_8M_gZRdY4g</recordid><startdate>20200825</startdate><enddate>20200825</enddate><creator>Lam, Yuko P. Y</creator><creator>Chiu, Cookson K. C</creator><creator>Wootton, Christopher A</creator><creator>Hands-Portman, Ian</creator><creator>Li, Meng</creator><creator>Barrow, Mark P</creator><creator>O'Connor, Peter B</creator><general>Royal Society of Chemistry</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>7SR</scope><scope>7U5</scope><scope>8BQ</scope><scope>8FD</scope><scope>JG9</scope><scope>L7M</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-6588-6274</orcidid><orcidid>https://orcid.org/0000-0001-6967-7675</orcidid><orcidid>https://orcid.org/0000-0002-6944-7009</orcidid><orcidid>https://orcid.org/0000-0002-8895-2342</orcidid><orcidid>https://orcid.org/0000-0002-6474-5357</orcidid><orcidid>https://orcid.org/0000-0002-3647-2611</orcidid><orcidid>https://orcid.org/0000-0001-5486-091X</orcidid></search><sort><creationdate>20200825</creationdate><title>Does deamidation affect inhibitory mechanisms towards amyloid protein aggregation?</title><author>Lam, Yuko P. Y ; Chiu, Cookson K. C ; Wootton, Christopher A ; Hands-Portman, Ian ; Li, Meng ; Barrow, Mark P ; O'Connor, Peter B</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c399t-f0bfd7cf6d274610071f1ba3e85c6077cf9763986de8791a92d53a8f7da23aa93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Amino Acid Sequence</topic><topic>Amyloid - chemistry</topic><topic>Amyloid - metabolism</topic><topic>Catechin - analogs & derivatives</topic><topic>Catechin - chemistry</topic><topic>Catechin - metabolism</topic><topic>Catechin - pharmacology</topic><topic>Humans</topic><topic>Inhibitors</topic><topic>Islet Amyloid Polypeptide - chemistry</topic><topic>Islet Amyloid Polypeptide - metabolism</topic><topic>Microscopy, Electron, Transmission</topic><topic>Protein Aggregates - drug effects</topic><topic>Proteins</topic><topic>Spectrometry, Fluorescence</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lam, Yuko P. Y</creatorcontrib><creatorcontrib>Chiu, Cookson K. C</creatorcontrib><creatorcontrib>Wootton, Christopher A</creatorcontrib><creatorcontrib>Hands-Portman, Ian</creatorcontrib><creatorcontrib>Li, Meng</creatorcontrib><creatorcontrib>Barrow, Mark P</creatorcontrib><creatorcontrib>O'Connor, Peter B</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Engineered Materials Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Materials Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>MEDLINE - Academic</collection><jtitle>Chemical communications (Cambridge, England)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lam, Yuko P. Y</au><au>Chiu, Cookson K. C</au><au>Wootton, Christopher A</au><au>Hands-Portman, Ian</au><au>Li, Meng</au><au>Barrow, Mark P</au><au>O'Connor, Peter B</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Does deamidation affect inhibitory mechanisms towards amyloid protein aggregation?</atitle><jtitle>Chemical communications (Cambridge, England)</jtitle><addtitle>Chem Commun (Camb)</addtitle><date>2020-08-25</date><risdate>2020</risdate><volume>56</volume><issue>68</issue><spage>9787</spage><epage>979</epage><pages>9787-979</pages><issn>1359-7345</issn><eissn>1364-548X</eissn><abstract>Deamidated amyloid proteins have been shown to accelerate fibril formation. Herein, the results show the inhibition performance and the interaction site between site-specific inhibitor and amyloid protein are significantly influenced by deamidation; while the inhibition mechanism of non-site specific inhibitor shows no significant disruption caused by amyloid protein deamidation.
A diagram to show the differences between wild-type and deamidated hIAPPs interaction with site specific and non-specific inhibitors.</abstract><cop>England</cop><pub>Royal Society of Chemistry</pub><pmid>32748913</pmid><doi>10.1039/d0cc03548c</doi><tpages>4</tpages><orcidid>https://orcid.org/0000-0002-6588-6274</orcidid><orcidid>https://orcid.org/0000-0001-6967-7675</orcidid><orcidid>https://orcid.org/0000-0002-6944-7009</orcidid><orcidid>https://orcid.org/0000-0002-8895-2342</orcidid><orcidid>https://orcid.org/0000-0002-6474-5357</orcidid><orcidid>https://orcid.org/0000-0002-3647-2611</orcidid><orcidid>https://orcid.org/0000-0001-5486-091X</orcidid><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 1359-7345 |
ispartof | Chemical communications (Cambridge, England), 2020-08, Vol.56 (68), p.9787-979 |
issn | 1359-7345 1364-548X |
language | eng |
recordid | cdi_crossref_primary_10_1039_D0CC03548C |
source | MEDLINE; Royal Society Of Chemistry Journals 2008-; Alma/SFX Local Collection |
subjects | Amino Acid Sequence Amyloid - chemistry Amyloid - metabolism Catechin - analogs & derivatives Catechin - chemistry Catechin - metabolism Catechin - pharmacology Humans Inhibitors Islet Amyloid Polypeptide - chemistry Islet Amyloid Polypeptide - metabolism Microscopy, Electron, Transmission Protein Aggregates - drug effects Proteins Spectrometry, Fluorescence |
title | Does deamidation affect inhibitory mechanisms towards amyloid protein aggregation? |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-10T02%3A45%3A55IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Does%20deamidation%20affect%20inhibitory%20mechanisms%20towards%20amyloid%20protein%20aggregation?&rft.jtitle=Chemical%20communications%20(Cambridge,%20England)&rft.au=Lam,%20Yuko%20P.%20Y&rft.date=2020-08-25&rft.volume=56&rft.issue=68&rft.spage=9787&rft.epage=979&rft.pages=9787-979&rft.issn=1359-7345&rft.eissn=1364-548X&rft_id=info:doi/10.1039/d0cc03548c&rft_dat=%3Cproquest_cross%3E2430372232%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2436864875&rft_id=info:pmid/32748913&rfr_iscdi=true |