Artificial Allosteric Receptors
Cooperative effects in the binding of two or more substrates to different binding sites of a receptor that are a result of a conformational change caused by the binding of the first substrate—also referred to as the effector—are called allosteric effects. In biological systems, allosteric regulation...
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Veröffentlicht in: | Chemistry : a European journal 2013-05, Vol.19 (20), p.6162-6196 |
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description | Cooperative effects in the binding of two or more substrates to different binding sites of a receptor that are a result of a conformational change caused by the binding of the first substrate—also referred to as the effector—are called allosteric effects. In biological systems, allosteric regulation is a widely used mechanism to control the function of proteins and enzymes in cellular metabolism. Inspired by this a lot of efforts have been made in supramolecular chemistry to implement this concept into artificial systems to control functions as molecular recognition, signal amplification, or even reactivity and catalysis. This review gives an up‐to‐date overview over the different approaches that have been reported ever since the first examples from the late 1970s/early 1980s. It covers both homo‐ and heterotropic examples and is divided according to the nature of the effector—cationic, anionic, or neutral—effectors and systems that use combinations of those.
Widely used: In biological systems, allosteric regulation is a widely used mechanism to control the function of proteins and enzymes. Inspired by this, a lot of effort has been made in supramolecular chemistry over the last 30 years to implement this concept into artificial systems to control functions such as molecular recognition, signal amplification, or even reactivity and catalysis, which are summarized here. |
doi_str_mv | 10.1002/chem.201203814 |
format | Article |
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Widely used: In biological systems, allosteric regulation is a widely used mechanism to control the function of proteins and enzymes. Inspired by this, a lot of effort has been made in supramolecular chemistry over the last 30 years to implement this concept into artificial systems to control functions such as molecular recognition, signal amplification, or even reactivity and catalysis, which are summarized here.</description><identifier>ISSN: 0947-6539</identifier><identifier>EISSN: 1521-3765</identifier><identifier>DOI: 10.1002/chem.201203814</identifier><identifier>PMID: 23463705</identifier><identifier>CODEN: CEUJED</identifier><language>eng</language><publisher>Weinheim: WILEY-VCH Verlag</publisher><subject>allosteric effects ; Allosteric Regulation ; Amplification ; Binding ; Binding Sites ; Catalysis ; Chemistry ; conformational switches ; Control ; Control systems ; cooperativity ; Enzymes ; Models, Chemical ; molecular recognition ; Proteins ; Proteins - chemistry ; Receptors ; Receptors, Artificial ; Recognition ; supramolecular chemistry</subject><ispartof>Chemistry : a European journal, 2013-05, Vol.19 (20), p.6162-6196</ispartof><rights>Copyright © 2013 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim</rights><rights>Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.</rights><rights>Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5474-5badabc8c0d288d0bcd1cac1fe025318ce13fd67ebc0e37a44abddf6bd867cd13</citedby><cites>FETCH-LOGICAL-c5474-5badabc8c0d288d0bcd1cac1fe025318ce13fd67ebc0e37a44abddf6bd867cd13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fchem.201203814$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fchem.201203814$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,27924,27925,45574,45575</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23463705$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kremer, Christopher</creatorcontrib><creatorcontrib>Lützen, Arne</creatorcontrib><title>Artificial Allosteric Receptors</title><title>Chemistry : a European journal</title><addtitle>Chem. Eur. J</addtitle><description>Cooperative effects in the binding of two or more substrates to different binding sites of a receptor that are a result of a conformational change caused by the binding of the first substrate—also referred to as the effector—are called allosteric effects. In biological systems, allosteric regulation is a widely used mechanism to control the function of proteins and enzymes in cellular metabolism. Inspired by this a lot of efforts have been made in supramolecular chemistry to implement this concept into artificial systems to control functions as molecular recognition, signal amplification, or even reactivity and catalysis. This review gives an up‐to‐date overview over the different approaches that have been reported ever since the first examples from the late 1970s/early 1980s. It covers both homo‐ and heterotropic examples and is divided according to the nature of the effector—cationic, anionic, or neutral—effectors and systems that use combinations of those.
Widely used: In biological systems, allosteric regulation is a widely used mechanism to control the function of proteins and enzymes. Inspired by this, a lot of effort has been made in supramolecular chemistry over the last 30 years to implement this concept into artificial systems to control functions such as molecular recognition, signal amplification, or even reactivity and catalysis, which are summarized here.</description><subject>allosteric effects</subject><subject>Allosteric Regulation</subject><subject>Amplification</subject><subject>Binding</subject><subject>Binding Sites</subject><subject>Catalysis</subject><subject>Chemistry</subject><subject>conformational switches</subject><subject>Control</subject><subject>Control systems</subject><subject>cooperativity</subject><subject>Enzymes</subject><subject>Models, Chemical</subject><subject>molecular recognition</subject><subject>Proteins</subject><subject>Proteins - chemistry</subject><subject>Receptors</subject><subject>Receptors, Artificial</subject><subject>Recognition</subject><subject>supramolecular chemistry</subject><issn>0947-6539</issn><issn>1521-3765</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0c1PwjAYBvDGaATRq0cl8eJl-LZdPzgSgmBETYxiwqXp2i4ON4btiPLfOwIS44VTL7_nSd6nCJ1j6GAAcmPeXdEhgAlQieMD1MSM4IgKzg5RE7qxiDij3QY6CWEGAF1O6TFqEBpzKoA10WXPV1mamUzn7V6el6FyPjPtZ2fcoip9OEVHqc6DO9u-LfR6O3jpj6Lx0_Cu3xtHhsUijliirU6MNGCJlBYSY7HRBqcOCKNYGodparlwiQFHhY5jnVib8sRKLmpLW-h607vw5efShUoVWTAuz_XclcugsBAS6jsF2U9pLBlQAFHTq390Vi79vD5krQSTAJLWqrNRxpcheJeqhc8K7VcKg1qvrNYrq93KdeBiW7tMCmd3_HfWGnQ34CvL3WpPneqPBg9_y6NNNqv_4nuX1f5DcUEFU2-PQzWZDqcT6BN1T38A07GWsA</recordid><startdate>20130510</startdate><enddate>20130510</enddate><creator>Kremer, Christopher</creator><creator>Lützen, Arne</creator><general>WILEY-VCH Verlag</general><general>WILEY‐VCH Verlag</general><general>Wiley Subscription Services, Inc</general><scope>BSCLL</scope><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>8BQ</scope><scope>8FD</scope><scope>JG9</scope><scope>K9.</scope><scope>7X8</scope></search><sort><creationdate>20130510</creationdate><title>Artificial Allosteric Receptors</title><author>Kremer, Christopher ; Lützen, Arne</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5474-5badabc8c0d288d0bcd1cac1fe025318ce13fd67ebc0e37a44abddf6bd867cd13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>allosteric effects</topic><topic>Allosteric Regulation</topic><topic>Amplification</topic><topic>Binding</topic><topic>Binding Sites</topic><topic>Catalysis</topic><topic>Chemistry</topic><topic>conformational switches</topic><topic>Control</topic><topic>Control systems</topic><topic>cooperativity</topic><topic>Enzymes</topic><topic>Models, Chemical</topic><topic>molecular recognition</topic><topic>Proteins</topic><topic>Proteins - chemistry</topic><topic>Receptors</topic><topic>Receptors, Artificial</topic><topic>Recognition</topic><topic>supramolecular chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kremer, Christopher</creatorcontrib><creatorcontrib>Lützen, Arne</creatorcontrib><collection>Istex</collection><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>METADEX</collection><collection>Technology Research Database</collection><collection>Materials Research Database</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>MEDLINE - Academic</collection><jtitle>Chemistry : a European journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kremer, Christopher</au><au>Lützen, Arne</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Artificial Allosteric Receptors</atitle><jtitle>Chemistry : a European journal</jtitle><addtitle>Chem. Eur. J</addtitle><date>2013-05-10</date><risdate>2013</risdate><volume>19</volume><issue>20</issue><spage>6162</spage><epage>6196</epage><pages>6162-6196</pages><issn>0947-6539</issn><eissn>1521-3765</eissn><coden>CEUJED</coden><abstract>Cooperative effects in the binding of two or more substrates to different binding sites of a receptor that are a result of a conformational change caused by the binding of the first substrate—also referred to as the effector—are called allosteric effects. In biological systems, allosteric regulation is a widely used mechanism to control the function of proteins and enzymes in cellular metabolism. Inspired by this a lot of efforts have been made in supramolecular chemistry to implement this concept into artificial systems to control functions as molecular recognition, signal amplification, or even reactivity and catalysis. This review gives an up‐to‐date overview over the different approaches that have been reported ever since the first examples from the late 1970s/early 1980s. It covers both homo‐ and heterotropic examples and is divided according to the nature of the effector—cationic, anionic, or neutral—effectors and systems that use combinations of those.
Widely used: In biological systems, allosteric regulation is a widely used mechanism to control the function of proteins and enzymes. Inspired by this, a lot of effort has been made in supramolecular chemistry over the last 30 years to implement this concept into artificial systems to control functions such as molecular recognition, signal amplification, or even reactivity and catalysis, which are summarized here.</abstract><cop>Weinheim</cop><pub>WILEY-VCH Verlag</pub><pmid>23463705</pmid><doi>10.1002/chem.201203814</doi><tpages>35</tpages></addata></record> |
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subjects | allosteric effects Allosteric Regulation Amplification Binding Binding Sites Catalysis Chemistry conformational switches Control Control systems cooperativity Enzymes Models, Chemical molecular recognition Proteins Proteins - chemistry Receptors Receptors, Artificial Recognition supramolecular chemistry |
title | Artificial Allosteric Receptors |
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