Aptamers and molecularly imprinted polymers as artificial biomimetic receptors in affinity capillary electrophoresis and electrochromatography
Identifieur interne : 002384 ( Istex/Corpus ); précédent : 002383; suivant : 002385Aptamers and molecularly imprinted polymers as artificial biomimetic receptors in affinity capillary electrophoresis and electrochromatography
Auteurs : Cristina Giovannoli ; Claudio Baggiani ; Laura Anfossi ; Gianfranco GiraudiSource :
- ELECTROPHORESIS [ 0173-0835 ] ; 2008-08.
English descriptors
- Teeft :
- Accurate determination, Affinity, Affinity capillary electrophoresis, Affinity probe, Affinity probes, Affinity studies, American chemical society, Amino acids, Anal, Analyte, Analyte concentration, Analytes, Analytical chemistry, Apce, Apce assay, Application fields, Aptamer, Aptamer applications, Aptamer binding, Aptamer collection window, Aptamer selection, Aptamers, Aptamers show, Artificial biomimetic receptors, Artificial receptors, Assay, Bare silica capillaries, Bare silica capillary, Berezovski, Binding ability, Binding behavior, Binding interactions, Binding parameters, Binding partners, Binding properties, Binding sequences, Biomedical fields, Bowser, Bubble formation, Buffer composition, Bulk polymer, Capillary, Capillary surface, Chem, Chromatogr, Competitive format, Complete separation, Complex formation, Different approach, Different kinds, Different target molecules, Dissociation constants, Drug deliv, Early example, Eceem, Electric field, Electrophoresis, Electrophoretic, Electrophoretic mobilities, Electrophoretic mobility, Electrophoretic patterns, Electrophoretic separation, Enantioseparation, Equilibrium mixture, Equilibrium mixtures, Experimental conditions, Exponential enrichment, First time, Flow cytometry, Free solution, Frit, Giovannoli, Gmbh, Haemin, High affinity, High affinity aptamers, High selectivity, High sensitivity, Important role, Imprinting, Inner surface, Kgaa, Koff, Krylov, Ligand, Ligand molecules, Limited amount, Mcgown, Mips, Mirror image, Mobility shift assay, Molecular imprinting, Molecular recognition mechanism, Molecular recognition properties, Molecular structures, Molecule, Monolithic capillaries, Muts protein, Nanoparticles, Natural receptors, Neceem, Neceem selection, Nilsson, Noncompetitive, Noncompetitive assay, Noncompetitive formats, Peak area, Peptide, Picomolar level, Polymer, Polymeric layer, Polymeric layers, Polymerization reaction, Porogenic, Porogenic solvents, Powerful tool, Predefined koff values, Preincubated, Preincubated samples, Prepolymerization mixture, Protein mixtures, Pseudostationary phase, Pseudostationary phases, Racemic phenylalanine, Random sequences, Reagent, Recent years, Receptor, Remcho, Ricin, Same approach, Same authors, Scanning electron micrographs, Schematic representation, Schweitz, Selective binding properties, Selective retention, Selectivity, Selex, Selex procedure, Separation conditions, Short analysis time, Silica, Similar affinities, Similar conditions, Small molecules, Smart aptamers, Solid phase, Specificity aptamers, Ssdna, Stationary, Stationary phase, Stationary phases, Systematic evolution, Target molecule, Target molecules, Template molecule, Theoretical treatment, Thermodynamic characterization, Thin layer, Typical features, Unbound, Unbound ones, Unbound sequences, Verlag, Verlag gmbh, Weinheim, Weinheim electrophoresis, Wide range.
Abstract
Artificial biomimetic receptors, such as aptamers and molecular‐imprinted polymers, show antibody‐like properties which are due to molecular recognition phenomena characterized by high affinity and selectivity. These binding features have made them suitable in all those application fields in which selective recognition is required. Thus, it is not surprising that they are finding applications in affinity CE as well. Recently, a variety of ACE methods have shown themselves to be suitable tools to provide a detailed quantitative characterization of the thermodynamic and kinetic aspects of binding. At the same time, affinity CE can exploit the peculiarities of these binding interactions to set up CE‐based analytical tools for the separation and the determination of specific target molecules in microscale formats. This review will provide a detailed description of affinity CE methods recently reported in the literature and related to these topics.
Url:
DOI: 10.1002/elps.200800004
Links to Exploration step
ISTEX:A5DB594F6D7F7B9E04CA1E587611528D6AA90FA2Le document en format XML
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Italy +39‐011‐6707615===</mods:affiliation></affiliation></author><author><name sortKey="Baggiani, Claudio" sort="Baggiani, Claudio" uniqKey="Baggiani C" first="Claudio" last="Baggiani">Claudio Baggiani</name><affiliation><mods:affiliation>Department of Analytical Chemistry, University of Torino, Torino, Italy</mods:affiliation></affiliation></author><author><name sortKey="Anfossi, Laura" sort="Anfossi, Laura" uniqKey="Anfossi L" first="Laura" last="Anfossi">Laura Anfossi</name><affiliation><mods:affiliation>Department of Analytical Chemistry, University of Torino, Torino, Italy</mods:affiliation></affiliation></author><author><name sortKey="Giraudi, Gianfranco" sort="Giraudi, Gianfranco" uniqKey="Giraudi G" first="Gianfranco" last="Giraudi">Gianfranco Giraudi</name><affiliation><mods:affiliation>Department of Analytical Chemistry, University of Torino, Torino, Italy</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j" type="main">ELECTROPHORESIS</title><title level="j" type="sub">Affinity and Immunoaffinity CE and CEC</title><title level="j" type="alt">ELECTROPHORESIS</title><idno type="ISSN">0173-0835</idno><idno type="eISSN">1522-2683</idno><imprint><biblScope unit="vol">29</biblScope><biblScope unit="issue">16</biblScope><biblScope unit="page" from="3349">3349</biblScope><biblScope unit="page" to="3365">3365</biblScope><biblScope unit="page-count">17</biblScope><publisher>WILEY‐VCH Verlag</publisher><pubPlace>Weinheim</pubPlace><date type="published" when="2008-08">2008-08</date></imprint><idno type="ISSN">0173-0835</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0173-0835</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Accurate determination</term><term>Affinity</term><term>Affinity capillary electrophoresis</term><term>Affinity probe</term><term>Affinity probes</term><term>Affinity studies</term><term>American chemical society</term><term>Amino acids</term><term>Anal</term><term>Analyte</term><term>Analyte concentration</term><term>Analytes</term><term>Analytical chemistry</term><term>Apce</term><term>Apce assay</term><term>Application fields</term><term>Aptamer</term><term>Aptamer applications</term><term>Aptamer binding</term><term>Aptamer collection window</term><term>Aptamer selection</term><term>Aptamers</term><term>Aptamers show</term><term>Artificial biomimetic receptors</term><term>Artificial receptors</term><term>Assay</term><term>Bare silica capillaries</term><term>Bare silica capillary</term><term>Berezovski</term><term>Binding ability</term><term>Binding behavior</term><term>Binding interactions</term><term>Binding parameters</term><term>Binding partners</term><term>Binding properties</term><term>Binding sequences</term><term>Biomedical fields</term><term>Bowser</term><term>Bubble formation</term><term>Buffer composition</term><term>Bulk polymer</term><term>Capillary</term><term>Capillary surface</term><term>Chem</term><term>Chromatogr</term><term>Competitive format</term><term>Complete separation</term><term>Complex formation</term><term>Different approach</term><term>Different kinds</term><term>Different target molecules</term><term>Dissociation constants</term><term>Drug deliv</term><term>Early example</term><term>Eceem</term><term>Electric field</term><term>Electrophoresis</term><term>Electrophoretic</term><term>Electrophoretic mobilities</term><term>Electrophoretic mobility</term><term>Electrophoretic patterns</term><term>Electrophoretic separation</term><term>Enantioseparation</term><term>Equilibrium mixture</term><term>Equilibrium mixtures</term><term>Experimental conditions</term><term>Exponential enrichment</term><term>First time</term><term>Flow cytometry</term><term>Free solution</term><term>Frit</term><term>Giovannoli</term><term>Gmbh</term><term>Haemin</term><term>High affinity</term><term>High affinity aptamers</term><term>High selectivity</term><term>High sensitivity</term><term>Important role</term><term>Imprinting</term><term>Inner surface</term><term>Kgaa</term><term>Koff</term><term>Krylov</term><term>Ligand</term><term>Ligand molecules</term><term>Limited amount</term><term>Mcgown</term><term>Mips</term><term>Mirror image</term><term>Mobility shift assay</term><term>Molecular imprinting</term><term>Molecular recognition mechanism</term><term>Molecular recognition properties</term><term>Molecular structures</term><term>Molecule</term><term>Monolithic capillaries</term><term>Muts protein</term><term>Nanoparticles</term><term>Natural receptors</term><term>Neceem</term><term>Neceem selection</term><term>Nilsson</term><term>Noncompetitive</term><term>Noncompetitive assay</term><term>Noncompetitive formats</term><term>Peak area</term><term>Peptide</term><term>Picomolar level</term><term>Polymer</term><term>Polymeric layer</term><term>Polymeric layers</term><term>Polymerization reaction</term><term>Porogenic</term><term>Porogenic solvents</term><term>Powerful tool</term><term>Predefined koff values</term><term>Preincubated</term><term>Preincubated samples</term><term>Prepolymerization mixture</term><term>Protein mixtures</term><term>Pseudostationary phase</term><term>Pseudostationary phases</term><term>Racemic phenylalanine</term><term>Random sequences</term><term>Reagent</term><term>Recent years</term><term>Receptor</term><term>Remcho</term><term>Ricin</term><term>Same approach</term><term>Same authors</term><term>Scanning electron micrographs</term><term>Schematic representation</term><term>Schweitz</term><term>Selective binding properties</term><term>Selective retention</term><term>Selectivity</term><term>Selex</term><term>Selex procedure</term><term>Separation conditions</term><term>Short analysis time</term><term>Silica</term><term>Similar affinities</term><term>Similar conditions</term><term>Small molecules</term><term>Smart aptamers</term><term>Solid phase</term><term>Specificity aptamers</term><term>Ssdna</term><term>Stationary</term><term>Stationary phase</term><term>Stationary phases</term><term>Systematic evolution</term><term>Target molecule</term><term>Target molecules</term><term>Template molecule</term><term>Theoretical treatment</term><term>Thermodynamic characterization</term><term>Thin layer</term><term>Typical features</term><term>Unbound</term><term>Unbound ones</term><term>Unbound sequences</term><term>Verlag</term><term>Verlag gmbh</term><term>Weinheim</term><term>Weinheim electrophoresis</term><term>Wide range</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Artificial biomimetic receptors, such as aptamers and molecular‐imprinted polymers, show antibody‐like properties which are due to molecular recognition phenomena characterized by high affinity and selectivity. These binding features have made them suitable in all those application fields in which selective recognition is required. Thus, it is not surprising that they are finding applications in affinity CE as well. Recently, a variety of ACE methods have shown themselves to be suitable tools to provide a detailed quantitative characterization of the thermodynamic and kinetic aspects of binding. At the same time, affinity CE can exploit the peculiarities of these binding interactions to set up CE‐based analytical tools for the separation and the determination of specific target molecules in microscale formats. This review will provide a detailed description of affinity CE methods recently reported in the literature and related to these topics.</div></front></TEI><istex><corpusName>wiley</corpusName><keywords><teeft><json:string>aptamers</json:string><json:string>chem</json:string><json:string>aptamer</json:string><json:string>receptor</json:string><json:string>anal</json:string><json:string>ssdna</json:string><json:string>nanoparticles</json:string><json:string>electrophoretic</json:string><json:string>weinheim</json:string><json:string>ricin</json:string><json:string>kgaa</json:string><json:string>verlag 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phenylalanine</json:string><json:string>important role</json:string><json:string>early example</json:string><json:string>same approach</json:string><json:string>bulk polymer</json:string><json:string>selective retention</json:string><json:string>binding ability</json:string><json:string>thin layer</json:string><json:string>selex procedure</json:string><json:string>first time</json:string><json:string>polymeric layer</json:string><json:string>polymeric layers</json:string><json:string>different kinds</json:string><json:string>analytical chemistry</json:string><json:string>polymerization reaction</json:string><json:string>porogenic solvents</json:string><json:string>scanning electron micrographs</json:string><json:string>unbound sequences</json:string><json:string>binding sequences</json:string><json:string>target molecules</json:string><json:string>preincubated samples</json:string><json:string>unbound ones</json:string><json:string>complex formation</json:string><json:string>systematic evolution</json:string><json:string>flow cytometry</json:string></teeft></keywords><author><json:item><name>Cristina Giovannoli Dr.</name><affiliations><json:string>Department of Analytical Chemistry, University of Torino, Torino, Italy</json:string><json:string>E-mail: cristina.giovannoli@unito.it</json:string><json:string>Correspondence address: Department of Analytical Chemistry, University of Torino, Via Giuria 5, I‐10125 Torino, Italy +39‐011‐6707615===</json:string></affiliations></json:item><json:item><name>Claudio Baggiani</name><affiliations><json:string>Department of Analytical Chemistry, University of Torino, Torino, Italy</json:string></affiliations></json:item><json:item><name>Laura Anfossi</name><affiliations><json:string>Department of Analytical Chemistry, University of Torino, Torino, Italy</json:string></affiliations></json:item><json:item><name>Gianfranco Giraudi</name><affiliations><json:string>Department of Analytical Chemistry, University of Torino, Torino, Italy</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>Affinity capillary electrophoresis</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Aptamers</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Biomimetic receptors</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Molecular imprinting</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Molecular recognition</value></json:item></subject><articleId><json:string>ELPS200800004</json:string></articleId><arkIstex>ark:/67375/WNG-WMM65T1C-J</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>reviewArticle</json:string></originalGenre><abstract>Artificial biomimetic receptors, such as aptamers and molecular‐imprinted polymers, show antibody‐like properties which are due to molecular recognition phenomena characterized by high affinity and selectivity. These binding features have made them suitable in all those application fields in which selective recognition is required. Thus, it is not surprising that they are finding applications in affinity CE as well. Recently, a variety of ACE methods have shown themselves to be suitable tools to provide a detailed quantitative characterization of the thermodynamic and kinetic aspects of binding. At the same time, affinity CE can exploit the peculiarities of these binding interactions to set up CE‐based analytical tools for the separation and the determination of specific target molecules in microscale formats. This review will provide a detailed description of affinity CE methods recently reported in the literature and related to these topics.</abstract><qualityIndicators><score>8.668</score><pdfWordCount>10052</pdfWordCount><pdfCharCount>65327</pdfCharCount><pdfVersion>1.3</pdfVersion><pdfPageCount>17</pdfPageCount><pdfPageSize>595.276 x 793.701 pts</pdfPageSize><pdfWordsPerPage>591</pdfWordsPerPage><pdfText>true</pdfText><refBibsNative>true</refBibsNative><abstractWordCount>139</abstractWordCount><abstractCharCount>957</abstractCharCount><keywordCount>5</keywordCount></qualityIndicators><title>Aptamers and molecularly imprinted polymers as artificial biomimetic receptors in affinity capillary electrophoresis and electrochromatography</title><pmid><json:string>18646281</json:string></pmid><genre><json:string>review-article</json:string></genre><host><title>ELECTROPHORESIS</title><language><json:string>unknown</json:string></language><doi><json:string>10.1002/(ISSN)1522-2683</json:string></doi><issn><json:string>0173-0835</json:string></issn><eissn><json:string>1522-2683</json:string></eissn><publisherId><json:string>ELPS</json:string></publisherId><volume>29</volume><issue>16</issue><pages><first>3349</first><last>3365</last><total>17</total></pages><genre><json:string>journal</json:string></genre><author><json:item><name>Terry M. Phillips</name></json:item></author><subject><json:item><value>CE and CEC</value></json:item><json:item><value>CE and CEC</value></json:item></subject></host><namedEntities><unitex><date><json:string>1990</json:string><json:string>2008</json:string><json:string>1980s</json:string></date><geogName></geogName><orgName><json:string>American Chemical Society</json:string><json:string>Department of Analytical Chemistry, University of Torino, Via Giuria</json:string></orgName><orgName_funder></orgName_funder><orgName_provider></orgName_provider><persName><json:string>Oligonucleotides</json:string><json:string>Electropherograms</json:string><json:string>Krylov</json:string></persName><placeName><json:string>LOD</json:string></placeName><ref_url></ref_url><ref_bibl><json:string>Ruta et al. [57]</json:string><json:string>[71, 72]</json:string><json:string>[34, 35]</json:string><json:string>[60]</json:string><json:string>[9, 44, 45]</json:string><json:string>Kotia et al. 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These binding features have made them suitable in all those application fields in which selective recognition is required. Thus, it is not surprising that they are finding applications in affinity CE as well. Recently, a variety of ACE methods have shown themselves to be suitable tools to provide a detailed quantitative characterization of the thermodynamic and kinetic aspects of binding. At the same time, affinity CE can exploit the peculiarities of these binding interactions to set up CE‐based analytical tools for the separation and the determination of specific target molecules in microscale formats. This review will provide a detailed description of affinity CE methods recently reported in the literature and related to these topics.</abstract><subject lang="en"><genre>keywords</genre><topic>Affinity capillary electrophoresis</topic><topic>Aptamers</topic><topic>Biomimetic receptors</topic><topic>Molecular imprinting</topic><topic>Molecular recognition</topic></subject><relatedItem type="host"><titleInfo><title>ELECTROPHORESIS</title></titleInfo><titleInfo type="abbreviated"><title>ELECTROPHORESIS</title></titleInfo><name type="personal"><namePart type="given">Terry M.</namePart><namePart type="family">Phillips</namePart></name><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><subject><genre>article-category</genre><topic>CE and CEC</topic><topic>CE and CEC</topic></subject><identifier type="ISSN">0173-0835</identifier><identifier type="eISSN">1522-2683</identifier><identifier type="DOI">10.1002/(ISSN)1522-2683</identifier><identifier type="PublisherID">ELPS</identifier><part><date>2008</date><detail type="title"><title>Affinity and Immunoaffinity CE and CEC</title></detail><detail type="volume"><caption>vol.</caption><number>29</number></detail><detail type="issue"><caption>no.</caption><number>16</number></detail><extent unit="pages"><start>3349</start><end>3365</end><total>17</total></extent></part></relatedItem><relatedItem type="references" displayLabel="cit1"><titleInfo><title>Angew. 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