Understanding and controlling the metal-directed assembly of terpyridine-functionalized coiled-coil peptides
Metal-binding peptides are versatile building blocks in supramolecular chemistry. We recently reported a class of crystalline materials formed through a combination of coiled-coil peptide self-association and metal coordination. Here, we probe the serendipitously discovered metal binding motif that...
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Veröffentlicht in: | Chemical communications (Cambridge, England) England), 2019-07, Vol.55 (54), p.7752-7755 |
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creator | Scheib, Kimberly A Tavenor, Nathan A Lawless, Matthew J Saxena, Sunil Horne, W. Seth |
description | Metal-binding peptides are versatile building blocks in supramolecular chemistry. We recently reported a class of crystalline materials formed through a combination of coiled-coil peptide self-association and metal coordination. Here, we probe the serendipitously discovered metal binding motif that drives the assembly and apply these insights to exert rational control over structure and morphology in the materials.
Spectroscopic elucidation of the interaction between terpyridine-functionalized coiled-coil peptides and Cu(
ii
) enables the construction of rationally designed supramolecular lattices. |
doi_str_mv | 10.1039/c9cc03496j |
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Spectroscopic elucidation of the interaction between terpyridine-functionalized coiled-coil peptides and Cu(
ii
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Spectroscopic elucidation of the interaction between terpyridine-functionalized coiled-coil peptides and Cu(
ii
) enables the construction of rationally designed supramolecular lattices.</description><subject>Amino Acid Motifs</subject><subject>Amino Acid Sequence</subject><subject>Assembly</subject><subject>Binding</subject><subject>Coils</subject><subject>Copper - chemistry</subject><subject>Electron Spin Resonance Spectroscopy - methods</subject><subject>Metalloproteins - chemical synthesis</subject><subject>Metalloproteins - chemistry</subject><subject>Morphology</subject><subject>Organic chemistry</subject><subject>Peptides</subject><subject>Protein Engineering - methods</subject><subject>Protein Multimerization</subject><subject>Pyridines - chemistry</subject><issn>1359-7345</issn><issn>1364-548X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkUlLxTAUhYMozhv3SsGNCNWkSTospTjywI2Cu5ImN5pHOpiki-evN_U5gNmchPvdc7k5CB0RfEEwrS5lJSWmrMqXG2iX0JylnJUvm_OdV2lBGd9Be94vcTyEl9toh5IMs4LSXWSfewXOB9Er078mURI59MEN1s7v8AZJB0HYVBkHMoBKhPfQtXaVDDoJ4MaVM7EVUj31MpihF9Z8wOxiLKh0lmSEMRgF_gBtaWE9HH7rPnq-uX6q79LF4-19fbVIJcM0pIJUeVYInhWqpAVRWlFWlpxqUrRQirZsc441IwBxG5brItd5RUiWcQ46Uy3dR2dr39EN7xP40HTGS7BW9DBMvokkIZjEYRE9_Ycuh8nFJb4ozAtalSRS52tKusF7B7oZnemEWzUEN3MGTV3V9VcGDxE--bac2g7UL_rz6RE4XgPOy9_qX4j0E2HujFc</recordid><startdate>20190702</startdate><enddate>20190702</enddate><creator>Scheib, Kimberly A</creator><creator>Tavenor, Nathan A</creator><creator>Lawless, Matthew J</creator><creator>Saxena, Sunil</creator><creator>Horne, W. Seth</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/0000-0002-3721-2942</orcidid><orcidid>https://orcid.org/0000-0001-9098-6114</orcidid><orcidid>https://orcid.org/0000-0003-2927-1739</orcidid></search><sort><creationdate>20190702</creationdate><title>Understanding and controlling the metal-directed assembly of terpyridine-functionalized coiled-coil peptides</title><author>Scheib, Kimberly A ; Tavenor, Nathan A ; Lawless, Matthew J ; Saxena, Sunil ; Horne, W. 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Seth</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Understanding and controlling the metal-directed assembly of terpyridine-functionalized coiled-coil peptides</atitle><jtitle>Chemical communications (Cambridge, England)</jtitle><addtitle>Chem Commun (Camb)</addtitle><date>2019-07-02</date><risdate>2019</risdate><volume>55</volume><issue>54</issue><spage>7752</spage><epage>7755</epage><pages>7752-7755</pages><issn>1359-7345</issn><eissn>1364-548X</eissn><abstract>Metal-binding peptides are versatile building blocks in supramolecular chemistry. We recently reported a class of crystalline materials formed through a combination of coiled-coil peptide self-association and metal coordination. Here, we probe the serendipitously discovered metal binding motif that drives the assembly and apply these insights to exert rational control over structure and morphology in the materials.
Spectroscopic elucidation of the interaction between terpyridine-functionalized coiled-coil peptides and Cu(
ii
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source | MEDLINE; Royal Society Of Chemistry Journals 2008-; Alma/SFX Local Collection |
subjects | Amino Acid Motifs Amino Acid Sequence Assembly Binding Coils Copper - chemistry Electron Spin Resonance Spectroscopy - methods Metalloproteins - chemical synthesis Metalloproteins - chemistry Morphology Organic chemistry Peptides Protein Engineering - methods Protein Multimerization Pyridines - chemistry |
title | Understanding and controlling the metal-directed assembly of terpyridine-functionalized coiled-coil peptides |
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