Optimization of a class of tryptophan dendrimers that inhibit HIV replication leads to a selective, specific, and low-nanomolar inhibitor of clinical isolates of enterovirus A71

Optimization of a class of tryptophan dendrimers that inhibit HIV replication leads to a selective, specific, and low-nanomolar inhibitor of clinical isolates of enterovirus A71

Tryptophan dendrimers that inhibit HIV replication by binding to the HIV envelope glycoproteins gp120 and gp41 have unexpectedly also proven to be potent, specific, and selective inhibitors of the replication of the unrelated enterovirus A71. Dendrimer 12, a consensus compound that was synthesized o...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Antimicrobial Agents and Chemotherapy 2016-08, Vol.60 (8), p.5064-5067
Hauptverfasser: Rivero-Buceta, Eva, Sun, Liang, Martínez-Gualda, Belén, Doyagüez, Elisa G, Donckers, Kim, Quesada, Ernesto, Camarasa, María-José, Delang, Leen, San-Félix, Ana, Neyts, Johan, Leyssen, Pieter
Format: Artikel
Sprache:eng
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 5067
container_issue 8
container_start_page 5064
container_title Antimicrobial Agents and Chemotherapy
container_volume 60
creator Rivero-Buceta, Eva
Sun, Liang
Martínez-Gualda, Belén
Doyagüez, Elisa G
Donckers, Kim
Quesada, Ernesto
Camarasa, María-José
Delang, Leen
San-Félix, Ana
Neyts, Johan
Leyssen, Pieter
description Tryptophan dendrimers that inhibit HIV replication by binding to the HIV envelope glycoproteins gp120 and gp41 have unexpectedly also proven to be potent, specific, and selective inhibitors of the replication of the unrelated enterovirus A71. Dendrimer 12, a consensus compound that was synthesized on the basis of the structure-activity relationship analysis of this series, is 3-fold more potent against the BrCr lab strain and, surprisingly, inhibits a large panel of clinical isolates in the low-nanomolar/high-picomolar range.
format Article
fullrecord <record><control><sourceid>kuleuven</sourceid><recordid>TN_cdi_kuleuven_dspace_123456789_546750</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>123456789_546750</sourcerecordid><originalsourceid>FETCH-kuleuven_dspace_123456789_5467503</originalsourceid><addsrcrecordid>eNqVjrtOxDAQRVOAxPL4h-ko2Ehe8totEQItFc2KNjL2RBlwbMszCY-_4g_J8uihmrmao3PnIFsoVdd5uVblUXbM_KTmXG3UIvu4j0IDvWuh4CF0oME4zbxfJb1FCbHXHix6m2jAxCC9FiDf0yMJbO8eIGF0ZL4FDrWdkTBrGB0aoQmXwBENdWSWoL0FF15yr30YgtPp1xTSvtE48rPKAfF8FPx6A71gChOlkeGqWZ1mh512jGc_8yQ7v73ZXW_z59HhOKFvLUdtsF1dFmVVN-tNW5V1U6niP-TF38hWXqX4BCpjcPY</addsrcrecordid><sourcetype>Institutional Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype></control><display><type>article</type><title>Optimization of a class of tryptophan dendrimers that inhibit HIV replication leads to a selective, specific, and low-nanomolar inhibitor of clinical isolates of enterovirus A71</title><source>Lirias (KU Leuven Association)</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>PubMed Central</source><creator>Rivero-Buceta, Eva ; Sun, Liang ; Martínez-Gualda, Belén ; Doyagüez, Elisa G ; Donckers, Kim ; Quesada, Ernesto ; Camarasa, María-José ; Delang, Leen ; San-Félix, Ana ; Neyts, Johan ; Leyssen, Pieter</creator><creatorcontrib>Rivero-Buceta, Eva ; Sun, Liang ; Martínez-Gualda, Belén ; Doyagüez, Elisa G ; Donckers, Kim ; Quesada, Ernesto ; Camarasa, María-José ; Delang, Leen ; San-Félix, Ana ; Neyts, Johan ; Leyssen, Pieter</creatorcontrib><description>Tryptophan dendrimers that inhibit HIV replication by binding to the HIV envelope glycoproteins gp120 and gp41 have unexpectedly also proven to be potent, specific, and selective inhibitors of the replication of the unrelated enterovirus A71. Dendrimer 12, a consensus compound that was synthesized on the basis of the structure-activity relationship analysis of this series, is 3-fold more potent against the BrCr lab strain and, surprisingly, inhibits a large panel of clinical isolates in the low-nanomolar/high-picomolar range.</description><identifier>ISSN: 0066-4804</identifier><language>eng</language><publisher>American Society for Microbiology (ASM)</publisher><ispartof>Antimicrobial Agents and Chemotherapy, 2016-08, Vol.60 (8), p.5064-5067</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,315,780,784,27860</link.rule.ids></links><search><creatorcontrib>Rivero-Buceta, Eva</creatorcontrib><creatorcontrib>Sun, Liang</creatorcontrib><creatorcontrib>Martínez-Gualda, Belén</creatorcontrib><creatorcontrib>Doyagüez, Elisa G</creatorcontrib><creatorcontrib>Donckers, Kim</creatorcontrib><creatorcontrib>Quesada, Ernesto</creatorcontrib><creatorcontrib>Camarasa, María-José</creatorcontrib><creatorcontrib>Delang, Leen</creatorcontrib><creatorcontrib>San-Félix, Ana</creatorcontrib><creatorcontrib>Neyts, Johan</creatorcontrib><creatorcontrib>Leyssen, Pieter</creatorcontrib><title>Optimization of a class of tryptophan dendrimers that inhibit HIV replication leads to a selective, specific, and low-nanomolar inhibitor of clinical isolates of enterovirus A71</title><title>Antimicrobial Agents and Chemotherapy</title><description>Tryptophan dendrimers that inhibit HIV replication by binding to the HIV envelope glycoproteins gp120 and gp41 have unexpectedly also proven to be potent, specific, and selective inhibitors of the replication of the unrelated enterovirus A71. Dendrimer 12, a consensus compound that was synthesized on the basis of the structure-activity relationship analysis of this series, is 3-fold more potent against the BrCr lab strain and, surprisingly, inhibits a large panel of clinical isolates in the low-nanomolar/high-picomolar range.</description><issn>0066-4804</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>FZOIL</sourceid><recordid>eNqVjrtOxDAQRVOAxPL4h-ko2Ehe8totEQItFc2KNjL2RBlwbMszCY-_4g_J8uihmrmao3PnIFsoVdd5uVblUXbM_KTmXG3UIvu4j0IDvWuh4CF0oME4zbxfJb1FCbHXHix6m2jAxCC9FiDf0yMJbO8eIGF0ZL4FDrWdkTBrGB0aoQmXwBENdWSWoL0FF15yr30YgtPp1xTSvtE48rPKAfF8FPx6A71gChOlkeGqWZ1mh512jGc_8yQ7v73ZXW_z59HhOKFvLUdtsF1dFmVVN-tNW5V1U6niP-TF38hWXqX4BCpjcPY</recordid><startdate>201608</startdate><enddate>201608</enddate><creator>Rivero-Buceta, Eva</creator><creator>Sun, Liang</creator><creator>Martínez-Gualda, Belén</creator><creator>Doyagüez, Elisa G</creator><creator>Donckers, Kim</creator><creator>Quesada, Ernesto</creator><creator>Camarasa, María-José</creator><creator>Delang, Leen</creator><creator>San-Félix, Ana</creator><creator>Neyts, Johan</creator><creator>Leyssen, Pieter</creator><general>American Society for Microbiology (ASM)</general><scope>FZOIL</scope></search><sort><creationdate>201608</creationdate><title>Optimization of a class of tryptophan dendrimers that inhibit HIV replication leads to a selective, specific, and low-nanomolar inhibitor of clinical isolates of enterovirus A71</title><author>Rivero-Buceta, Eva ; Sun, Liang ; Martínez-Gualda, Belén ; Doyagüez, Elisa G ; Donckers, Kim ; Quesada, Ernesto ; Camarasa, María-José ; Delang, Leen ; San-Félix, Ana ; Neyts, Johan ; Leyssen, Pieter</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-kuleuven_dspace_123456789_5467503</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rivero-Buceta, Eva</creatorcontrib><creatorcontrib>Sun, Liang</creatorcontrib><creatorcontrib>Martínez-Gualda, Belén</creatorcontrib><creatorcontrib>Doyagüez, Elisa G</creatorcontrib><creatorcontrib>Donckers, Kim</creatorcontrib><creatorcontrib>Quesada, Ernesto</creatorcontrib><creatorcontrib>Camarasa, María-José</creatorcontrib><creatorcontrib>Delang, Leen</creatorcontrib><creatorcontrib>San-Félix, Ana</creatorcontrib><creatorcontrib>Neyts, Johan</creatorcontrib><creatorcontrib>Leyssen, Pieter</creatorcontrib><collection>Lirias (KU Leuven Association)</collection><jtitle>Antimicrobial Agents and Chemotherapy</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rivero-Buceta, Eva</au><au>Sun, Liang</au><au>Martínez-Gualda, Belén</au><au>Doyagüez, Elisa G</au><au>Donckers, Kim</au><au>Quesada, Ernesto</au><au>Camarasa, María-José</au><au>Delang, Leen</au><au>San-Félix, Ana</au><au>Neyts, Johan</au><au>Leyssen, Pieter</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Optimization of a class of tryptophan dendrimers that inhibit HIV replication leads to a selective, specific, and low-nanomolar inhibitor of clinical isolates of enterovirus A71</atitle><jtitle>Antimicrobial Agents and Chemotherapy</jtitle><date>2016-08</date><risdate>2016</risdate><volume>60</volume><issue>8</issue><spage>5064</spage><epage>5067</epage><pages>5064-5067</pages><issn>0066-4804</issn><abstract>Tryptophan dendrimers that inhibit HIV replication by binding to the HIV envelope glycoproteins gp120 and gp41 have unexpectedly also proven to be potent, specific, and selective inhibitors of the replication of the unrelated enterovirus A71. Dendrimer 12, a consensus compound that was synthesized on the basis of the structure-activity relationship analysis of this series, is 3-fold more potent against the BrCr lab strain and, surprisingly, inhibits a large panel of clinical isolates in the low-nanomolar/high-picomolar range.</abstract><pub>American Society for Microbiology (ASM)</pub></addata></record>
fulltext fulltext
identifier ISSN: 0066-4804
ispartof Antimicrobial Agents and Chemotherapy, 2016-08, Vol.60 (8), p.5064-5067
issn 0066-4804
language eng
recordid cdi_kuleuven_dspace_123456789_546750
source Lirias (KU Leuven Association); Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central
title Optimization of a class of tryptophan dendrimers that inhibit HIV replication leads to a selective, specific, and low-nanomolar inhibitor of clinical isolates of enterovirus A71
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-04T08%3A06%3A54IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-kuleuven&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Optimization%20of%20a%20class%20of%20tryptophan%20dendrimers%20that%20inhibit%20HIV%20replication%20leads%20to%20a%20selective,%20specific,%20and%20low-nanomolar%20inhibitor%20of%20clinical%20isolates%20of%20enterovirus%20A71&rft.jtitle=Antimicrobial%20Agents%20and%20Chemotherapy&rft.au=Rivero-Buceta,%20Eva&rft.date=2016-08&rft.volume=60&rft.issue=8&rft.spage=5064&rft.epage=5067&rft.pages=5064-5067&rft.issn=0066-4804&rft_id=info:doi/&rft_dat=%3Ckuleuven%3E123456789_546750%3C/kuleuven%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_id=info:pmid/&rfr_iscdi=true