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Directional assembly of a stapled α-helical peptide
The de novo design of stapled peptide-based self-assemblies attracts vast interest, yet still remains challenging. The development of an oxidation trigger for peptide stapling and subsequent self-assembly is described here. A self-assembling sequence, Fmoc-R(RCEX) 2 -NH 2 , transformed from a random...
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| Published in: | Chemical communications (Cambridge, England) England), 2019-08, Vol.55 (7), p.1484-1487 |
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| Main Authors: | , , , , , , , , |
| Format: | Article |
| Language: | English |
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| cited_by | cdi_FETCH-LOGICAL-c337t-9f8579fc1f5fa205a5b9980cf2b7e0a86fdc95220501433aee628bc09658ce173 |
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| cites | cdi_FETCH-LOGICAL-c337t-9f8579fc1f5fa205a5b9980cf2b7e0a86fdc95220501433aee628bc09658ce173 |
| container_end_page | 1487 |
| container_issue | 7 |
| container_start_page | 1484 |
| container_title | Chemical communications (Cambridge, England) |
| container_volume | 55 |
| creator | Hu, Kuan Yin, Feng Zhou, Ziyuan Lian, Chenshan Liu, Yinghuan Sun, Chengjie Li, Wenjun Zhang, Jianing Li, Zigang |
| description | The
de novo
design of stapled peptide-based self-assemblies attracts vast interest, yet still remains challenging. The development of an oxidation trigger for peptide stapling and subsequent self-assembly is described here. A self-assembling sequence, Fmoc-R(RCEX)
2
-NH
2
, transformed from a random coil to an α-helical structure upon disulphide bonding of the flanking cysteine residues positioning at the
i
/
i
+ 4 locations. The stapling form of this peptide enforces a conformational restraint that affords the driving force for self-assembly into nanorod/nanovesicle structures. Moreover, these assembled materials can transport siRNA into cancer cells and immediately release the cargo in a reductive environment.
In this work, we described a method to control the helical peptide self-assembly by stapling the peptide
via
an intramolecular disulfide bridge. |
| doi_str_mv | 10.1039/c9cc04591k |
| format | article |
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de novo
design of stapled peptide-based self-assemblies attracts vast interest, yet still remains challenging. The development of an oxidation trigger for peptide stapling and subsequent self-assembly is described here. A self-assembling sequence, Fmoc-R(RCEX)
2
-NH
2
, transformed from a random coil to an α-helical structure upon disulphide bonding of the flanking cysteine residues positioning at the
i
/
i
+ 4 locations. The stapling form of this peptide enforces a conformational restraint that affords the driving force for self-assembly into nanorod/nanovesicle structures. Moreover, these assembled materials can transport siRNA into cancer cells and immediately release the cargo in a reductive environment.
In this work, we described a method to control the helical peptide self-assembly by stapling the peptide
via
an intramolecular disulfide bridge.</description><identifier>ISSN: 1359-7345</identifier><identifier>EISSN: 1364-548X</identifier><identifier>DOI: 10.1039/c9cc04591k</identifier><identifier>PMID: 31414101</identifier><language>eng</language><publisher>England: Royal Society of Chemistry</publisher><subject>Assembling ; Coils ; Microscopy, Atomic Force ; Nanorods ; Oxidation ; Oxidation-Reduction ; Peptides ; Peptides - chemistry ; Protein Conformation, alpha-Helical ; Self-assembly</subject><ispartof>Chemical communications (Cambridge, England), 2019-08, Vol.55 (7), p.1484-1487</ispartof><rights>Copyright Royal Society of Chemistry 2019</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c337t-9f8579fc1f5fa205a5b9980cf2b7e0a86fdc95220501433aee628bc09658ce173</citedby><cites>FETCH-LOGICAL-c337t-9f8579fc1f5fa205a5b9980cf2b7e0a86fdc95220501433aee628bc09658ce173</cites><orcidid>0000-0003-2448-2254 ; 0000-0002-4649-1592 ; 0000-0001-7407-9047</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/31414101$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hu, Kuan</creatorcontrib><creatorcontrib>Yin, Feng</creatorcontrib><creatorcontrib>Zhou, Ziyuan</creatorcontrib><creatorcontrib>Lian, Chenshan</creatorcontrib><creatorcontrib>Liu, Yinghuan</creatorcontrib><creatorcontrib>Sun, Chengjie</creatorcontrib><creatorcontrib>Li, Wenjun</creatorcontrib><creatorcontrib>Zhang, Jianing</creatorcontrib><creatorcontrib>Li, Zigang</creatorcontrib><title>Directional assembly of a stapled α-helical peptide</title><title>Chemical communications (Cambridge, England)</title><addtitle>Chem Commun (Camb)</addtitle><description>The
de novo
design of stapled peptide-based self-assemblies attracts vast interest, yet still remains challenging. The development of an oxidation trigger for peptide stapling and subsequent self-assembly is described here. A self-assembling sequence, Fmoc-R(RCEX)
2
-NH
2
, transformed from a random coil to an α-helical structure upon disulphide bonding of the flanking cysteine residues positioning at the
i
/
i
+ 4 locations. The stapling form of this peptide enforces a conformational restraint that affords the driving force for self-assembly into nanorod/nanovesicle structures. Moreover, these assembled materials can transport siRNA into cancer cells and immediately release the cargo in a reductive environment.
In this work, we described a method to control the helical peptide self-assembly by stapling the peptide
via
an intramolecular disulfide bridge.</description><subject>Assembling</subject><subject>Coils</subject><subject>Microscopy, Atomic Force</subject><subject>Nanorods</subject><subject>Oxidation</subject><subject>Oxidation-Reduction</subject><subject>Peptides</subject><subject>Peptides - chemistry</subject><subject>Protein Conformation, alpha-Helical</subject><subject>Self-assembly</subject><issn>1359-7345</issn><issn>1364-548X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><recordid>eNpd0c9LwzAUB_AgipvTi3el4EWEatIkTXIc9ScOvCh4K2n6gp3tWpP2sD_Lf8S_yczNCeYdEngfHuT7EDom-JJgqq6MMgYzrsj7DhoTmrKYM_m6u3pzFQvK-AgdeD_H4RAu99GIEhYKkzFi15UD01ftQteR9h6aol5GrY105Hvd1VBGX5_xG9SVCaCDrq9KOER7Vtcejjb3BL3c3jxn9_Hs6e4hm85iQ6noY2UlF8oaYrnVCeaaF0pJbGxSCMBaprY0iiehgwmjVAOkiSwMVimXBoigE3S-ntu59mMA3-dN5Q3UtV5AO_g8SQQVEguMAz37R-ft4MKnVkpixohKk6Au1sq41nsHNu9c1Wi3zAnOV1nmmcqynywfAz7djByKBsot_Q0vgJM1cN5su3_LoN_sdnbl</recordid><startdate>20190827</startdate><enddate>20190827</enddate><creator>Hu, Kuan</creator><creator>Yin, Feng</creator><creator>Zhou, Ziyuan</creator><creator>Lian, Chenshan</creator><creator>Liu, Yinghuan</creator><creator>Sun, Chengjie</creator><creator>Li, Wenjun</creator><creator>Zhang, Jianing</creator><creator>Li, Zigang</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/0000-0003-2448-2254</orcidid><orcidid>https://orcid.org/0000-0002-4649-1592</orcidid><orcidid>https://orcid.org/0000-0001-7407-9047</orcidid></search><sort><creationdate>20190827</creationdate><title>Directional assembly of a stapled α-helical peptide</title><author>Hu, Kuan ; Yin, Feng ; Zhou, Ziyuan ; Lian, Chenshan ; Liu, Yinghuan ; Sun, Chengjie ; Li, Wenjun ; Zhang, Jianing ; Li, Zigang</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c337t-9f8579fc1f5fa205a5b9980cf2b7e0a86fdc95220501433aee628bc09658ce173</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2019</creationdate><topic>Assembling</topic><topic>Coils</topic><topic>Microscopy, Atomic Force</topic><topic>Nanorods</topic><topic>Oxidation</topic><topic>Oxidation-Reduction</topic><topic>Peptides</topic><topic>Peptides - chemistry</topic><topic>Protein Conformation, alpha-Helical</topic><topic>Self-assembly</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hu, Kuan</creatorcontrib><creatorcontrib>Yin, Feng</creatorcontrib><creatorcontrib>Zhou, Ziyuan</creatorcontrib><creatorcontrib>Lian, Chenshan</creatorcontrib><creatorcontrib>Liu, Yinghuan</creatorcontrib><creatorcontrib>Sun, Chengjie</creatorcontrib><creatorcontrib>Li, Wenjun</creatorcontrib><creatorcontrib>Zhang, Jianing</creatorcontrib><creatorcontrib>Li, Zigang</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>Hu, Kuan</au><au>Yin, Feng</au><au>Zhou, Ziyuan</au><au>Lian, Chenshan</au><au>Liu, Yinghuan</au><au>Sun, Chengjie</au><au>Li, Wenjun</au><au>Zhang, Jianing</au><au>Li, Zigang</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Directional assembly of a stapled α-helical peptide</atitle><jtitle>Chemical communications (Cambridge, England)</jtitle><addtitle>Chem Commun (Camb)</addtitle><date>2019-08-27</date><risdate>2019</risdate><volume>55</volume><issue>7</issue><spage>1484</spage><epage>1487</epage><pages>1484-1487</pages><issn>1359-7345</issn><eissn>1364-548X</eissn><abstract>The
de novo
design of stapled peptide-based self-assemblies attracts vast interest, yet still remains challenging. The development of an oxidation trigger for peptide stapling and subsequent self-assembly is described here. A self-assembling sequence, Fmoc-R(RCEX)
2
-NH
2
, transformed from a random coil to an α-helical structure upon disulphide bonding of the flanking cysteine residues positioning at the
i
/
i
+ 4 locations. The stapling form of this peptide enforces a conformational restraint that affords the driving force for self-assembly into nanorod/nanovesicle structures. Moreover, these assembled materials can transport siRNA into cancer cells and immediately release the cargo in a reductive environment.
In this work, we described a method to control the helical peptide self-assembly by stapling the peptide
via
an intramolecular disulfide bridge.</abstract><cop>England</cop><pub>Royal Society of Chemistry</pub><pmid>31414101</pmid><doi>10.1039/c9cc04591k</doi><tpages>4</tpages><orcidid>https://orcid.org/0000-0003-2448-2254</orcidid><orcidid>https://orcid.org/0000-0002-4649-1592</orcidid><orcidid>https://orcid.org/0000-0001-7407-9047</orcidid></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1359-7345 |
| ispartof | Chemical communications (Cambridge, England), 2019-08, Vol.55 (7), p.1484-1487 |
| issn | 1359-7345 1364-548X |
| language | eng |
| recordid | cdi_rsc_primary_c9cc04591k |
| source | Royal Society of Chemistry |
| subjects | Assembling Coils Microscopy, Atomic Force Nanorods Oxidation Oxidation-Reduction Peptides Peptides - chemistry Protein Conformation, alpha-Helical Self-assembly |
| title | Directional assembly of a stapled α-helical peptide |
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