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Turning electron transfer ‘on-off’ in peptides through side-bridge gating
[Display omitted] Electrochemical studies are reported on a series of peptides to determine the influence of different side-chains and backbone rigidity on electron transfer, to progress the field of molecular electronics. Specifically, these peptides share either a common helical or β-strand confor...
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| Published in: | Electrochimica acta 2016-08, Vol.209, p.65-74 |
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| Language: | English |
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| cites | cdi_FETCH-LOGICAL-c434t-952d7484d8df624a8cda0e260159f6c3d569ef48d8290924f3eff15390552cc13 |
| container_end_page | 74 |
| container_issue | |
| container_start_page | 65 |
| container_title | Electrochimica acta |
| container_volume | 209 |
| creator | Yu, Jingxian Horsley, John R. Abell, Andrew D. |
| description | [Display omitted]
Electrochemical studies are reported on a series of peptides to determine the influence of different side-chains and backbone rigidity on electron transfer, to progress the field of molecular electronics. Specifically, these peptides share either a common helical or β-strand conformation to cover a range of secondary structures, to fully investigate the influence of backbone rigidity. Two types of side-chain tethers, either triazole-containing or alkene-containing, are also compared to investigate these effects on electron transfer. Our results showed that the observed formal potentials (Eo) and electron transfer rate constants (ket) fall into two distinct groups. The peptides constrained via a side-chain tether exhibited high formal potentials and low electron transfer rate constants, whereas the linear peptides displayed low formal potentials and high electron transfer rate constants. This was found to occur irrespective of the backbone conformation, or the nature of the side-chain constraint. The vast formal potential shifts (as much as 482mV) and the large disparity in the electron transfer rate constants (as much as 97%) between the constrained and linear peptides, provides two distinct states (i.e. on/off) with a sizeable differential, which is ideal for the design of molecular switches. |
| doi_str_mv | 10.1016/j.electacta.2016.05.067 |
| format | article |
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Electrochemical studies are reported on a series of peptides to determine the influence of different side-chains and backbone rigidity on electron transfer, to progress the field of molecular electronics. Specifically, these peptides share either a common helical or β-strand conformation to cover a range of secondary structures, to fully investigate the influence of backbone rigidity. Two types of side-chain tethers, either triazole-containing or alkene-containing, are also compared to investigate these effects on electron transfer. Our results showed that the observed formal potentials (Eo) and electron transfer rate constants (ket) fall into two distinct groups. The peptides constrained via a side-chain tether exhibited high formal potentials and low electron transfer rate constants, whereas the linear peptides displayed low formal potentials and high electron transfer rate constants. This was found to occur irrespective of the backbone conformation, or the nature of the side-chain constraint. The vast formal potential shifts (as much as 482mV) and the large disparity in the electron transfer rate constants (as much as 97%) between the constrained and linear peptides, provides two distinct states (i.e. on/off) with a sizeable differential, which is ideal for the design of molecular switches.</description><identifier>ISSN: 0013-4686</identifier><identifier>EISSN: 1873-3859</identifier><identifier>DOI: 10.1016/j.electacta.2016.05.067</identifier><language>eng</language><publisher>Elsevier Ltd</publisher><subject>310-helical ; Backbone ; Click chemistry ; Constraints ; Electron transfer ; Electron transfer in peptides ; Gating and risering ; Peptides ; Rate constants ; Rigidity ; Ring-closing metathesis ; Side-bridge ; Tethers ; β-strand</subject><ispartof>Electrochimica acta, 2016-08, Vol.209, p.65-74</ispartof><rights>2016 Elsevier Ltd</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c434t-952d7484d8df624a8cda0e260159f6c3d569ef48d8290924f3eff15390552cc13</citedby><cites>FETCH-LOGICAL-c434t-952d7484d8df624a8cda0e260159f6c3d569ef48d8290924f3eff15390552cc13</cites><orcidid>0000-0002-6489-5988</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,786,790,27957,27958</link.rule.ids></links><search><creatorcontrib>Yu, Jingxian</creatorcontrib><creatorcontrib>Horsley, John R.</creatorcontrib><creatorcontrib>Abell, Andrew D.</creatorcontrib><title>Turning electron transfer ‘on-off’ in peptides through side-bridge gating</title><title>Electrochimica acta</title><description>[Display omitted]
Electrochemical studies are reported on a series of peptides to determine the influence of different side-chains and backbone rigidity on electron transfer, to progress the field of molecular electronics. Specifically, these peptides share either a common helical or β-strand conformation to cover a range of secondary structures, to fully investigate the influence of backbone rigidity. Two types of side-chain tethers, either triazole-containing or alkene-containing, are also compared to investigate these effects on electron transfer. Our results showed that the observed formal potentials (Eo) and electron transfer rate constants (ket) fall into two distinct groups. The peptides constrained via a side-chain tether exhibited high formal potentials and low electron transfer rate constants, whereas the linear peptides displayed low formal potentials and high electron transfer rate constants. This was found to occur irrespective of the backbone conformation, or the nature of the side-chain constraint. The vast formal potential shifts (as much as 482mV) and the large disparity in the electron transfer rate constants (as much as 97%) between the constrained and linear peptides, provides two distinct states (i.e. on/off) with a sizeable differential, which is ideal for the design of molecular switches.</description><subject>310-helical</subject><subject>Backbone</subject><subject>Click chemistry</subject><subject>Constraints</subject><subject>Electron transfer</subject><subject>Electron transfer in peptides</subject><subject>Gating and risering</subject><subject>Peptides</subject><subject>Rate constants</subject><subject>Rigidity</subject><subject>Ring-closing metathesis</subject><subject>Side-bridge</subject><subject>Tethers</subject><subject>β-strand</subject><issn>0013-4686</issn><issn>1873-3859</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><recordid>eNqFkM1KAzEQx4MoWKvP4B697DrZfGz2WIpfUPFSz2FNJtuUdrcmW8Gbj6Gv1ycxteJVGBhm-M8P5kfIJYWCApXXywJXaIYmVVGmRQGiAFkdkRFVFcuZEvUxGQFQlnOp5Ck5i3EJAJWsYEQe59vQ-a7NfiCh77IhNF10GLLdx2ff5b1zu4-vzHfZBjeDtxizYRH6bbvIYpryl-Bti1nbDIlyTk5cs4p48dvH5Pn2Zj69z2dPdw_TySw3nPEhr0VpK664VdbJkjfK2AawlEBF7aRhVsgaHVdWlTXUJXcMnaOC1SBEaQxlY3J14G5C_7rFOOi1jwZXq6bDfhs1VUxIDpTLFK0OURP6GAM6vQl-3YR3TUHvBeql_hOo9wI1CJ0EpsvJ4RLTJ28eg47GY2fQ-pDy2vb-X8Y3JaB_pg</recordid><startdate>20160810</startdate><enddate>20160810</enddate><creator>Yu, Jingxian</creator><creator>Horsley, John R.</creator><creator>Abell, Andrew D.</creator><general>Elsevier Ltd</general><scope>AAYXX</scope><scope>CITATION</scope><scope>7SR</scope><scope>7U5</scope><scope>8BQ</scope><scope>8FD</scope><scope>JG9</scope><scope>L7M</scope><orcidid>https://orcid.org/0000-0002-6489-5988</orcidid></search><sort><creationdate>20160810</creationdate><title>Turning electron transfer ‘on-off’ in peptides through side-bridge gating</title><author>Yu, Jingxian ; Horsley, John R. ; Abell, Andrew D.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c434t-952d7484d8df624a8cda0e260159f6c3d569ef48d8290924f3eff15390552cc13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>310-helical</topic><topic>Backbone</topic><topic>Click chemistry</topic><topic>Constraints</topic><topic>Electron transfer</topic><topic>Electron transfer in peptides</topic><topic>Gating and risering</topic><topic>Peptides</topic><topic>Rate constants</topic><topic>Rigidity</topic><topic>Ring-closing metathesis</topic><topic>Side-bridge</topic><topic>Tethers</topic><topic>β-strand</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yu, Jingxian</creatorcontrib><creatorcontrib>Horsley, John R.</creatorcontrib><creatorcontrib>Abell, Andrew D.</creatorcontrib><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><jtitle>Electrochimica acta</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yu, Jingxian</au><au>Horsley, John R.</au><au>Abell, Andrew D.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Turning electron transfer ‘on-off’ in peptides through side-bridge gating</atitle><jtitle>Electrochimica acta</jtitle><date>2016-08-10</date><risdate>2016</risdate><volume>209</volume><spage>65</spage><epage>74</epage><pages>65-74</pages><issn>0013-4686</issn><eissn>1873-3859</eissn><notes>ObjectType-Article-1</notes><notes>SourceType-Scholarly Journals-1</notes><notes>ObjectType-Feature-2</notes><notes>content type line 23</notes><abstract>[Display omitted]
Electrochemical studies are reported on a series of peptides to determine the influence of different side-chains and backbone rigidity on electron transfer, to progress the field of molecular electronics. Specifically, these peptides share either a common helical or β-strand conformation to cover a range of secondary structures, to fully investigate the influence of backbone rigidity. Two types of side-chain tethers, either triazole-containing or alkene-containing, are also compared to investigate these effects on electron transfer. Our results showed that the observed formal potentials (Eo) and electron transfer rate constants (ket) fall into two distinct groups. The peptides constrained via a side-chain tether exhibited high formal potentials and low electron transfer rate constants, whereas the linear peptides displayed low formal potentials and high electron transfer rate constants. This was found to occur irrespective of the backbone conformation, or the nature of the side-chain constraint. The vast formal potential shifts (as much as 482mV) and the large disparity in the electron transfer rate constants (as much as 97%) between the constrained and linear peptides, provides two distinct states (i.e. on/off) with a sizeable differential, which is ideal for the design of molecular switches.</abstract><pub>Elsevier Ltd</pub><doi>10.1016/j.electacta.2016.05.067</doi><tpages>10</tpages><orcidid>https://orcid.org/0000-0002-6489-5988</orcidid><oa>free_for_read</oa></addata></record> |
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| ispartof | Electrochimica acta, 2016-08, Vol.209, p.65-74 |
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| language | eng |
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| source | ScienceDirect Freedom Collection 2022-2024 |
| subjects | 310-helical Backbone Click chemistry Constraints Electron transfer Electron transfer in peptides Gating and risering Peptides Rate constants Rigidity Ring-closing metathesis Side-bridge Tethers β-strand |
| title | Turning electron transfer ‘on-off’ in peptides through side-bridge gating |
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