Site-specific Isopeptide Bridge Tethering of Chimeric gp41 N-terminal Heptad Repeat Helical Trimers for the Treatment of HIV-1 Infection
Peptides derived from the N-terminal heptad repeat (NHR) of HIV-1 gp41 can be potent inhibitors against viral entry when presented in a nonaggregating trimeric coiled-coil conformation via the introduction of exogenous trimerization motifs and intermolecular disulfide bonds. We recently discovered t...
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| Veröffentlicht in: | Scientific reports 2016-08, Vol.6 (1), p.32161, Article 32161 |
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| creator | Wang, Chao Li, Xue Yu, Fei Lu, Lu Jiang, Xifeng Xu, Xiaoyu Wang, Huixin Lai, Wenqing Zhang, Tianhong Zhang, Zhenqing Ye, Ling Jiang, Shibo Liu, Keliang |
| description | Peptides derived from the N-terminal heptad repeat (NHR) of HIV-1 gp41 can be potent inhibitors against viral entry when presented in a nonaggregating trimeric coiled-coil conformation via the introduction of exogenous trimerization motifs and intermolecular disulfide bonds. We recently discovered that crosslinking isopeptide bridges within the
de novo
helical trimers added exceptional resistance to unfolding. Herein, we attempted to optimize (CCIZN17)
3
, a representative disulfide bond-stabilized chimeric NHR-trimer, by incorporating site-specific interhelical isopeptide bonds as the redox-sensitive disulfide surrogate. In this process, we systematically examined the effect of isopeptide bond position and molecular sizes of auxiliary trimeric coiled-coil motif and NHR fragments on the antiviral potency of these NHR-trimers. Pleasingly, (IZ14N24N)
3
possessed promising inhibitory activity against HIV-1 infection and markedly increased proteolytic stability relative to its disulfide-tethered counterpart, suggesting good potential for further development as an effective antiviral agent for treatment of HIV-1 infection. |
| doi_str_mv | 10.1038/srep32161 |
| format | Article |
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de novo
helical trimers added exceptional resistance to unfolding. Herein, we attempted to optimize (CCIZN17)
3
, a representative disulfide bond-stabilized chimeric NHR-trimer, by incorporating site-specific interhelical isopeptide bonds as the redox-sensitive disulfide surrogate. In this process, we systematically examined the effect of isopeptide bond position and molecular sizes of auxiliary trimeric coiled-coil motif and NHR fragments on the antiviral potency of these NHR-trimers. Pleasingly, (IZ14N24N)
3
possessed promising inhibitory activity against HIV-1 infection and markedly increased proteolytic stability relative to its disulfide-tethered counterpart, suggesting good potential for further development as an effective antiviral agent for treatment of HIV-1 infection.</description><identifier>ISSN: 2045-2322</identifier><identifier>EISSN: 2045-2322</identifier><identifier>DOI: 10.1038/srep32161</identifier><identifier>PMID: 27562370</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>631/154/309/2420 ; 692/699/255/1901 ; 82/16 ; Amino Acid Motifs ; Animals ; Antiviral Agents - chemistry ; Antiviral Agents - pharmacology ; Cell Line ; Chemical bonds ; Conformation ; Disulfide bonds ; Glycoprotein gp41 ; HIV Envelope Protein gp41 - chemistry ; HIV Envelope Protein gp41 - pharmacology ; HIV Infections - drug therapy ; HIV Infections - metabolism ; HIV Infections - pathology ; HIV-1 - metabolism ; Humanities and Social Sciences ; Humans ; Infections ; Male ; multidisciplinary ; Peptides ; Peptides - chemistry ; Peptides - pharmacology ; Proteolysis ; Rats ; Rats, Sprague-Dawley ; Science</subject><ispartof>Scientific reports, 2016-08, Vol.6 (1), p.32161, Article 32161</ispartof><rights>The Author(s) 2016</rights><rights>Copyright Nature Publishing Group Aug 2016</rights><rights>Copyright © 2016, The Author(s) 2016 The Author(s)</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c438t-2bbe81f33b37b765d6b9704f4c7f93911ac4ee75e2a5efab53ae63e79efc171a3</citedby><cites>FETCH-LOGICAL-c438t-2bbe81f33b37b765d6b9704f4c7f93911ac4ee75e2a5efab53ae63e79efc171a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4999862/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4999862/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,27923,27924,41119,42188,51575,53790,53792</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27562370$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wang, Chao</creatorcontrib><creatorcontrib>Li, Xue</creatorcontrib><creatorcontrib>Yu, Fei</creatorcontrib><creatorcontrib>Lu, Lu</creatorcontrib><creatorcontrib>Jiang, Xifeng</creatorcontrib><creatorcontrib>Xu, Xiaoyu</creatorcontrib><creatorcontrib>Wang, Huixin</creatorcontrib><creatorcontrib>Lai, Wenqing</creatorcontrib><creatorcontrib>Zhang, Tianhong</creatorcontrib><creatorcontrib>Zhang, Zhenqing</creatorcontrib><creatorcontrib>Ye, Ling</creatorcontrib><creatorcontrib>Jiang, Shibo</creatorcontrib><creatorcontrib>Liu, Keliang</creatorcontrib><title>Site-specific Isopeptide Bridge Tethering of Chimeric gp41 N-terminal Heptad Repeat Helical Trimers for the Treatment of HIV-1 Infection</title><title>Scientific reports</title><addtitle>Sci Rep</addtitle><addtitle>Sci Rep</addtitle><description>Peptides derived from the N-terminal heptad repeat (NHR) of HIV-1 gp41 can be potent inhibitors against viral entry when presented in a nonaggregating trimeric coiled-coil conformation via the introduction of exogenous trimerization motifs and intermolecular disulfide bonds. We recently discovered that crosslinking isopeptide bridges within the
de novo
helical trimers added exceptional resistance to unfolding. Herein, we attempted to optimize (CCIZN17)
3
, a representative disulfide bond-stabilized chimeric NHR-trimer, by incorporating site-specific interhelical isopeptide bonds as the redox-sensitive disulfide surrogate. In this process, we systematically examined the effect of isopeptide bond position and molecular sizes of auxiliary trimeric coiled-coil motif and NHR fragments on the antiviral potency of these NHR-trimers. Pleasingly, (IZ14N24N)
3
possessed promising inhibitory activity against HIV-1 infection and markedly increased proteolytic stability relative to its disulfide-tethered counterpart, suggesting good potential for further development as an effective antiviral agent for treatment of HIV-1 infection.</description><subject>631/154/309/2420</subject><subject>692/699/255/1901</subject><subject>82/16</subject><subject>Amino Acid Motifs</subject><subject>Animals</subject><subject>Antiviral Agents - chemistry</subject><subject>Antiviral Agents - pharmacology</subject><subject>Cell Line</subject><subject>Chemical bonds</subject><subject>Conformation</subject><subject>Disulfide bonds</subject><subject>Glycoprotein gp41</subject><subject>HIV Envelope Protein gp41 - chemistry</subject><subject>HIV Envelope Protein gp41 - pharmacology</subject><subject>HIV Infections - drug therapy</subject><subject>HIV Infections - metabolism</subject><subject>HIV Infections - pathology</subject><subject>HIV-1 - metabolism</subject><subject>Humanities and Social Sciences</subject><subject>Humans</subject><subject>Infections</subject><subject>Male</subject><subject>multidisciplinary</subject><subject>Peptides</subject><subject>Peptides - 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chemistry</topic><topic>Antiviral Agents - pharmacology</topic><topic>Cell Line</topic><topic>Chemical bonds</topic><topic>Conformation</topic><topic>Disulfide bonds</topic><topic>Glycoprotein gp41</topic><topic>HIV Envelope Protein gp41 - chemistry</topic><topic>HIV Envelope Protein gp41 - pharmacology</topic><topic>HIV Infections - drug therapy</topic><topic>HIV Infections - metabolism</topic><topic>HIV Infections - pathology</topic><topic>HIV-1 - metabolism</topic><topic>Humanities and Social Sciences</topic><topic>Humans</topic><topic>Infections</topic><topic>Male</topic><topic>multidisciplinary</topic><topic>Peptides</topic><topic>Peptides - chemistry</topic><topic>Peptides - pharmacology</topic><topic>Proteolysis</topic><topic>Rats</topic><topic>Rats, Sprague-Dawley</topic><topic>Science</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wang, Chao</creatorcontrib><creatorcontrib>Li, Xue</creatorcontrib><creatorcontrib>Yu, Fei</creatorcontrib><creatorcontrib>Lu, Lu</creatorcontrib><creatorcontrib>Jiang, Xifeng</creatorcontrib><creatorcontrib>Xu, Xiaoyu</creatorcontrib><creatorcontrib>Wang, Huixin</creatorcontrib><creatorcontrib>Lai, Wenqing</creatorcontrib><creatorcontrib>Zhang, Tianhong</creatorcontrib><creatorcontrib>Zhang, Zhenqing</creatorcontrib><creatorcontrib>Ye, Ling</creatorcontrib><creatorcontrib>Jiang, Shibo</creatorcontrib><creatorcontrib>Liu, Keliang</creatorcontrib><collection>Springer Nature OA Free Journals</collection><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>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</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>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Biological Science Database</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 Basic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Scientific reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wang, Chao</au><au>Li, Xue</au><au>Yu, Fei</au><au>Lu, Lu</au><au>Jiang, Xifeng</au><au>Xu, Xiaoyu</au><au>Wang, Huixin</au><au>Lai, Wenqing</au><au>Zhang, Tianhong</au><au>Zhang, Zhenqing</au><au>Ye, Ling</au><au>Jiang, Shibo</au><au>Liu, Keliang</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Site-specific Isopeptide Bridge Tethering of Chimeric gp41 N-terminal Heptad Repeat Helical Trimers for the Treatment of HIV-1 Infection</atitle><jtitle>Scientific reports</jtitle><stitle>Sci Rep</stitle><addtitle>Sci Rep</addtitle><date>2016-08-26</date><risdate>2016</risdate><volume>6</volume><issue>1</issue><spage>32161</spage><pages>32161-</pages><artnum>32161</artnum><issn>2045-2322</issn><eissn>2045-2322</eissn><abstract>Peptides derived from the N-terminal heptad repeat (NHR) of HIV-1 gp41 can be potent inhibitors against viral entry when presented in a nonaggregating trimeric coiled-coil conformation via the introduction of exogenous trimerization motifs and intermolecular disulfide bonds. We recently discovered that crosslinking isopeptide bridges within the
de novo
helical trimers added exceptional resistance to unfolding. Herein, we attempted to optimize (CCIZN17)
3
, a representative disulfide bond-stabilized chimeric NHR-trimer, by incorporating site-specific interhelical isopeptide bonds as the redox-sensitive disulfide surrogate. In this process, we systematically examined the effect of isopeptide bond position and molecular sizes of auxiliary trimeric coiled-coil motif and NHR fragments on the antiviral potency of these NHR-trimers. Pleasingly, (IZ14N24N)
3
possessed promising inhibitory activity against HIV-1 infection and markedly increased proteolytic stability relative to its disulfide-tethered counterpart, suggesting good potential for further development as an effective antiviral agent for treatment of HIV-1 infection.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>27562370</pmid><doi>10.1038/srep32161</doi><oa>free_for_read</oa></addata></record> |
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| subjects | 631/154/309/2420 692/699/255/1901 82/16 Amino Acid Motifs Animals Antiviral Agents - chemistry Antiviral Agents - pharmacology Cell Line Chemical bonds Conformation Disulfide bonds Glycoprotein gp41 HIV Envelope Protein gp41 - chemistry HIV Envelope Protein gp41 - pharmacology HIV Infections - drug therapy HIV Infections - metabolism HIV Infections - pathology HIV-1 - metabolism Humanities and Social Sciences Humans Infections Male multidisciplinary Peptides Peptides - chemistry Peptides - pharmacology Proteolysis Rats Rats, Sprague-Dawley Science |
| title | Site-specific Isopeptide Bridge Tethering of Chimeric gp41 N-terminal Heptad Repeat Helical Trimers for the Treatment of HIV-1 Infection |
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