Coherent membrane supports for parallel microsynthesis and screening of bioactive peptides
Identifieur interne : 003755 ( Main/Exploration ); précédent : 003754; suivant : 003756Coherent membrane supports for parallel microsynthesis and screening of bioactive peptides
Auteurs : Holger Wenschuh [Allemagne] ; Rudolf Volkmer-Engert [Allemagne] ; Margit Schmidt [Allemagne] ; Marco Schulz [Allemagne] ; Jens Schneider-Mergener [Allemagne] ; Ulrich Reineke [Allemagne]Source :
- Peptide Science [ 0006-3525 ] ; 2000.
English descriptors
- Teeft :
- Acid, Acrylic acid, Acrylic acid methylester, Akademiai kiado, Amino, Amino acid, Amino acids, Amino functionalization, Amino functionalized, Amino functionalized cellulose membrane, Amino functionalized cellulose membranes, Amino functions, Ammonia vapor, Antibody epitopes, Antigenic determinants, Antimicrobial peptides, Assay, Binding assays, Binding regions, Binding sites, Bioactive peptides, Biol, Biol chem, Biological assays, Biomedical research, Cellulose, Cellulose membrane, Cellulose membranes, Cellulose surface, Chem, Chem lett, Cleavage, Coherent membrane, Combinat chem, Combinatorial, Combinatorial libraries, Compound libraries, Covalent linkage, Czech chem commun, Deprotection steps, Different loadings, Discontinuous epitope, Epitope, Epitope mapping, Ester, European peptide symposium, Febs lett, Functionalization, Functionalized, General scheme, Germeroth, Gmbh, Groups monomer, High throughput, Hydroxy, Hydroxy functions, Immunol, John wiley sons, Kramer, Large numbers, Lett, Linear epitopes, Linker, Linker systems, Maximum loading, Mechanical stability, Medizinische immunologie, Membrane, Membrane functionalization, Membrane support, Membrane surface, Methylester, Microtiter plates, Monomer, Monomer concentration, Novel screening assays, Nucleic acids, Parallel synthesis, Pept protein, Peptide, Peptide acid, Peptide amide, Peptide epitopes, Peptide libraries, Peptide membranes, Peptide release, Peptide scan, Peptide synthesis, Perchloric acid, Photoinduced graft copolymerization, Polyclonal serum, Polymeric membranes, Polypropylene, Polypropylene membranes, Proc natl acad, Protease solution, Randomized, Randomized position, Randomized positions, Reactive groups, Recent developments, Reineke, Robot, Rudower chaussee, Same time, Screening, Screening assays, Solid phase synthesis, Solid support, Solvent systems, Subsequent screening, Such binding regions, Surface hydrophilicity, Technik gmbh, Tetrahedron, Tetrahedron lett, Tools gmbh, Valuable tool, Verlag gmbh, Wenschuh.
Abstract
Since its invention the SPOT‐synthesis methodology has become one of the most efficient strategies for the miniaturized assembly of large numbers of peptides. The combination of a facile synthetic method with high throughput solid‐ and solution‐phase screening assays qualifies the SPOT‐technique as a valuable tool in biomedical research. Recent developments such as the introduction of novel polymeric surfaces, new linker and cleavage strategies as well as automated robot systems extended the scope of practical chemical reactions that can be accommodated as well as the numbers of compounds obtainable by this technique. Thus, highly complex spatially addressed compound arrays have become accessible. Together with the introduction of novel screening assays, the method is excellently suited to elucidate recognition events on the molecular level. © 2000 John Wiley & Sons, Inc. Biopolymers (Pept Sci) 55: 188–206, 2000
Url:
DOI: 10.1002/1097-0282(2000)55:3<188::AID-BIP20>3.0.CO;2-T
Affiliations:
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type="ISSN">0006-3525</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0006-3525</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Acid</term><term>Acrylic acid</term><term>Acrylic acid methylester</term><term>Akademiai kiado</term><term>Amino</term><term>Amino acid</term><term>Amino acids</term><term>Amino functionalization</term><term>Amino functionalized</term><term>Amino functionalized cellulose membrane</term><term>Amino functionalized cellulose membranes</term><term>Amino functions</term><term>Ammonia vapor</term><term>Antibody epitopes</term><term>Antigenic determinants</term><term>Antimicrobial peptides</term><term>Assay</term><term>Binding assays</term><term>Binding regions</term><term>Binding sites</term><term>Bioactive peptides</term><term>Biol</term><term>Biol chem</term><term>Biological assays</term><term>Biomedical research</term><term>Cellulose</term><term>Cellulose membrane</term><term>Cellulose membranes</term><term>Cellulose surface</term><term>Chem</term><term>Chem lett</term><term>Cleavage</term><term>Coherent membrane</term><term>Combinat chem</term><term>Combinatorial</term><term>Combinatorial libraries</term><term>Compound libraries</term><term>Covalent linkage</term><term>Czech chem commun</term><term>Deprotection steps</term><term>Different loadings</term><term>Discontinuous epitope</term><term>Epitope</term><term>Epitope mapping</term><term>Ester</term><term>European peptide symposium</term><term>Febs lett</term><term>Functionalization</term><term>Functionalized</term><term>General scheme</term><term>Germeroth</term><term>Gmbh</term><term>Groups monomer</term><term>High throughput</term><term>Hydroxy</term><term>Hydroxy functions</term><term>Immunol</term><term>John wiley sons</term><term>Kramer</term><term>Large numbers</term><term>Lett</term><term>Linear epitopes</term><term>Linker</term><term>Linker systems</term><term>Maximum loading</term><term>Mechanical stability</term><term>Medizinische immunologie</term><term>Membrane</term><term>Membrane functionalization</term><term>Membrane support</term><term>Membrane surface</term><term>Methylester</term><term>Microtiter plates</term><term>Monomer</term><term>Monomer concentration</term><term>Novel screening assays</term><term>Nucleic acids</term><term>Parallel synthesis</term><term>Pept protein</term><term>Peptide</term><term>Peptide acid</term><term>Peptide amide</term><term>Peptide epitopes</term><term>Peptide libraries</term><term>Peptide membranes</term><term>Peptide release</term><term>Peptide scan</term><term>Peptide synthesis</term><term>Perchloric acid</term><term>Photoinduced graft copolymerization</term><term>Polyclonal serum</term><term>Polymeric membranes</term><term>Polypropylene</term><term>Polypropylene membranes</term><term>Proc natl acad</term><term>Protease solution</term><term>Randomized</term><term>Randomized position</term><term>Randomized positions</term><term>Reactive groups</term><term>Recent developments</term><term>Reineke</term><term>Robot</term><term>Rudower chaussee</term><term>Same time</term><term>Screening</term><term>Screening assays</term><term>Solid phase synthesis</term><term>Solid support</term><term>Solvent systems</term><term>Subsequent screening</term><term>Such binding regions</term><term>Surface hydrophilicity</term><term>Technik gmbh</term><term>Tetrahedron</term><term>Tetrahedron lett</term><term>Tools gmbh</term><term>Valuable tool</term><term>Verlag gmbh</term><term>Wenschuh</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Since its invention the SPOT‐synthesis methodology has become one of the most efficient strategies for the miniaturized assembly of large numbers of peptides. The combination of a facile synthetic method with high throughput solid‐ and solution‐phase screening assays qualifies the SPOT‐technique as a valuable tool in biomedical research. Recent developments such as the introduction of novel polymeric surfaces, new linker and cleavage strategies as well as automated robot systems extended the scope of practical chemical reactions that can be accommodated as well as the numbers of compounds obtainable by this technique. Thus, highly complex spatially addressed compound arrays have become accessible. Together with the introduction of novel screening assays, the method is excellently suited to elucidate recognition events on the molecular level. © 2000 John Wiley & Sons, Inc. Biopolymers (Pept Sci) 55: 188–206, 2000</div></front></TEI><affiliations><list><country><li>Allemagne</li></country><region><li>Berlin</li></region><settlement><li>Berlin</li></settlement></list><tree><country name="Allemagne"><region name="Berlin"><name sortKey="Wenschuh, Holger" sort="Wenschuh, Holger" uniqKey="Wenschuh H" first="Holger" last="Wenschuh">Holger Wenschuh</name></region><name sortKey="Reineke, Ulrich" sort="Reineke, Ulrich" uniqKey="Reineke U" first="Ulrich" last="Reineke">Ulrich Reineke</name><name sortKey="Schmidt, Margit" sort="Schmidt, Margit" uniqKey="Schmidt M" first="Margit" last="Schmidt">Margit Schmidt</name><name sortKey="Schneider Ergener, Jens" sort="Schneider Ergener, Jens" uniqKey="Schneider Ergener J" first="Jens" last="Schneider-Mergener">Jens Schneider-Mergener</name><name sortKey="Schulz, Marco" sort="Schulz, Marco" uniqKey="Schulz M" first="Marco" last="Schulz">Marco Schulz</name><name sortKey="Volkmer Ngert, Rudolf" sort="Volkmer Ngert, Rudolf" uniqKey="Volkmer Ngert R" first="Rudolf" last="Volkmer-Engert">Rudolf Volkmer-Engert</name><name sortKey="Wenschuh, Holger" sort="Wenschuh, Holger" uniqKey="Wenschuh H" first="Holger" last="Wenschuh">Holger Wenschuh</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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