Multiple Peptide Synthesis Methods and Their Applications. New Synthetic Methods (87)
Identifieur interne : 002451 ( Istex/Corpus ); précédent : 002450; suivant : 002452Multiple Peptide Synthesis Methods and Their Applications. New Synthetic Methods (87)
Auteurs : Günther Jung ; Annette G. Beck-SickingerSource :
- Angewandte Chemie International Edition in English [ 0570-0833 ] ; 1992-04.
English descriptors
- Teeft :
- Acid, Acrylic acid, Active peptide, Active peptides, Amino, Amino acid, Amino acid derivatives, Amino acid mixtures, Amino acids, Analogue, Analytical procedures, Anchor positions, Angew, Batsberg pedersen, Biochem, Biological activities, Biological activity, Biological test system, Biological tests, Chain lengths, Chem, Circular dichroism measurements, Cleavage, Computer program, Conformational mapping, Corresponding acid, Definite positions, Deprotection, Deres, Different peptides, Elisa, Engl, Epitope, Epitope mapping, Escom, First time, Flow rate, Flow synthesizer, Fmoc, Fmoc strategy, Free peptides, Gruyter, High performance, Hormone analogues, Houghten, Hplc, Individual peptides, Instrumental analysis, Jung, Killer cells, Large number, Larger peptides, Leiden, Many peptides, Mass spectrometry, Merrifield, Metzger, Modern methods, Molecular level, Monoclonal, Monoclonal antibodies, Monoclonal antibody, Multiple cleavage, Multiple methods, Multiple peptide analysis, Multiple peptide synthesis, Multiple peptide synthesis methods, Multiple synthesis, Multiple synthesis methods, Novel lantibiotics, Organic chemistry, Paper disks, Parallel synthesis, Pept, Peptide, Peptide chemist, Peptide chemistry, Peptide libraries, Peptide mixture, Peptide mixtures, Peptide numbers, Peptide sequences, Peptide solutions, Peptide synthesis, Personal computer, Phage, Pipetting, Pipetting robots, Pmol, Polyclonal sera, Polyethylene film, Polyethylene rods, Polymer, Polymeric, Polymeric beads, Polymeric support, Positive sera, Proc, Protein chemistry, Protein research foundation, Protein segments, Rammensee, Rapid development, Reaction vessel, Reaction vessels, Reagent, Receptor, Robot, Schematic representation, Schnorrenberg, Secondary structure, Several positions, Short peptides, Short time, Simultaneous preparation, Small amounts, Solid phase peptide synthesis, Solid phase synthesis, Soluble receptors screening, Such peptides, Suction, Symp, Synthesis, Synthesizer, Synthetic cycle, Synthetic peptides, Tbtu, Tbtu tetrafluoroborate, Tetrahedron lett, Trifluoroacetic acid, Tubingen, Universitat tubingen, Vaccine, Variable positions, Wiesmiiller, Zinsser smps.
Abstract
Rapid developments in the biotechnology of new proteins, as well as advances in immunology and the development of pharmaceuticals based on inhibitors and antagonists, have led to immense demands for synthetic peptides. Simultaneous preparation of 100–150 completely different peptides, having chain lengths of up to 20 amino acids can nowadays be achieved using multiple synthesis methods. The yields and qualities of the peptides so obtained are high enough to permit reliable in vivo and in vitro screening for biological activities. Moreover, it is possible to optimize synthetic conditions and to carry out comparative studies on the secondary structures and conformational mapping of proteins. Special multiple synthesis methods facilitate the epitope mapping of larger peptides for diagnostic purposes and for the development of vaccines based on a few hundreds of free or rod‐bound peptides that are useful for immunoassays. Multiple methods of peptide synthesis also enable the preparation of so‐called peptide libraries which could comprise hundreds of thousands of peptides, and by which new perspectives for the screening of lead structures will be opened up. Peptide synthesis using a combination of photolabile protecting groups and photolithographic procedures enables the assembling of peptide libraries on small plates for use in miniature immunoassays. Furthermore, lipopeptide‐antigen conjugates allow both the preparation of peptide‐specific and monoclonal antibodies as well as a complete screening of epitopes of B‐, T‐helper and T‐killer cells. Applications in the areas of AIDS diagnosis, the development of vaccines, and screening for the hormone analogues, demonstrate just some of the possibilities that have been opened up by multiple peptide synthesis methods.
Peptide fishing is a new sport in bioorganic and medicinal chemistry–biologically active peptides are identified from an ocean of peptides of various lengths and constitutions. In the last few years new methods have been developed for the synthesis of such peptide collections. Automation is the next step. For example, in immuno‐analysis the pin method is very important. Minute amounts of peptide are synthesized on rods (a few hundred simultaneously) and incubated with sera containing antibodies for the analysis. In this way the relevant epitopes, that is, the regions to which the antibodies bind, can be precisely determined and mapped.
Url:
DOI: 10.1002/anie.199203673
Links to Exploration step
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<front><div type="abstract" xml:lang="en">Rapid developments in the biotechnology of new proteins, as well as advances in immunology and the development of pharmaceuticals based on inhibitors and antagonists, have led to immense demands for synthetic peptides. Simultaneous preparation of 100–150 completely different peptides, having chain lengths of up to 20 amino acids can nowadays be achieved using multiple synthesis methods. The yields and qualities of the peptides so obtained are high enough to permit reliable in vivo and in vitro screening for biological activities. Moreover, it is possible to optimize synthetic conditions and to carry out comparative studies on the secondary structures and conformational mapping of proteins. Special multiple synthesis methods facilitate the epitope mapping of larger peptides for diagnostic purposes and for the development of vaccines based on a few hundreds of free or rod‐bound peptides that are useful for immunoassays. Multiple methods of peptide synthesis also enable the preparation of so‐called peptide libraries which could comprise hundreds of thousands of peptides, and by which new perspectives for the screening of lead structures will be opened up. Peptide synthesis using a combination of photolabile protecting groups and photolithographic procedures enables the assembling of peptide libraries on small plates for use in miniature immunoassays. Furthermore, lipopeptide‐antigen conjugates allow both the preparation of peptide‐specific and monoclonal antibodies as well as a complete screening of epitopes of B‐, T‐helper and T‐killer cells. Applications in the areas of AIDS diagnosis, the development of vaccines, and screening for the hormone analogues, demonstrate just some of the possibilities that have been opened up by multiple peptide synthesis methods.</div>
<div type="abstract" xml:lang="en">Peptide fishing is a new sport in bioorganic and medicinal chemistry–biologically active peptides are identified from an ocean of peptides of various lengths and constitutions. In the last few years new methods have been developed for the synthesis of such peptide collections. Automation is the next step. For example, in immuno‐analysis the pin method is very important. Minute amounts of peptide are synthesized on rods (a few hundred simultaneously) and incubated with sera containing antibodies for the analysis. In this way the relevant epitopes, that is, the regions to which the antibodies bind, can be precisely determined and mapped.</div>
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<p>Rapid developments in the biotechnology of new proteins, as well as advances in immunology and the development of pharmaceuticals based on inhibitors and antagonists, have led to immense demands for synthetic peptides. Simultaneous preparation of 100–150 completely different peptides, having chain lengths of up to 20 amino acids can nowadays be achieved using multiple synthesis methods. The yields and qualities of the peptides so obtained are high enough to permit reliable in vivo and in vitro screening for biological activities. Moreover, it is possible to optimize synthetic conditions and to carry out comparative studies on the secondary structures and conformational mapping of proteins. Special multiple synthesis methods facilitate the epitope mapping of larger peptides for diagnostic purposes and for the development of vaccines based on a few hundreds of free or rod‐bound peptides that are useful for immunoassays. Multiple methods of peptide synthesis also enable the preparation of so‐called peptide libraries which could comprise hundreds of thousands of peptides, and by which new perspectives for the screening of lead structures will be opened up. Peptide synthesis using a combination of photolabile protecting groups and photolithographic procedures enables the assembling of peptide libraries on small plates for use in miniature immunoassays. Furthermore, lipopeptide‐antigen conjugates allow both the preparation of peptide‐specific and monoclonal antibodies as well as a complete screening of epitopes of B‐, T‐helper and T‐killer cells. Applications in the areas of AIDS diagnosis, the development of vaccines, and screening for the hormone analogues, demonstrate just some of the possibilities that have been opened up by multiple peptide synthesis methods.</p>
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<abstract xml:lang="en" style="short"><p><hi rend="bold">Peptide fishing</hi>
is a new sport in bioorganic and medicinal chemistry–biologically active peptides are identified from an ocean of peptides of various lengths and constitutions. In the last few years new methods have been developed for the synthesis of such peptide collections. Automation is the next step. For example, in immuno‐analysis the pin method is very important. Minute amounts of peptide are synthesized on rods (a few hundred simultaneously) and incubated with sera containing antibodies for the analysis. In this way the relevant epitopes, that is, the regions to which the antibodies bind, can be precisely determined and mapped.</p>
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<p>Rapid developments in the biotechnology of new proteins, as well as advances in immunology and the development of pharmaceuticals based on inhibitors and antagonists, have led to immense demands for synthetic peptides. Simultaneous preparation of 100–150 completely different peptides, having chain lengths of up to 20 amino acids can nowadays be achieved using multiple synthesis methods. The yields and qualities of the peptides so obtained are high enough to permit reliable in vivo and in vitro screening for biological activities. Moreover, it is possible to optimize synthetic conditions and to carry out comparative studies on the secondary structures and conformational mapping of proteins. Special multiple synthesis methods facilitate the epitope mapping of larger peptides for diagnostic purposes and for the development of vaccines based on a few hundreds of free or rod‐bound peptides that are useful for immunoassays. Multiple methods of peptide synthesis also enable the preparation of so‐called peptide libraries which could comprise hundreds of thousands of peptides, and by which new perspectives for the screening of lead structures will be opened up. Peptide synthesis using a combination of photolabile protecting groups and photolithographic procedures enables the assembling of peptide libraries on small plates for use in miniature immunoassays. Furthermore, lipopeptide‐antigen conjugates allow both the preparation of peptide‐specific and monoclonal antibodies as well as a complete screening of epitopes of B‐, T‐helper and T‐killer cells. Applications in the areas of AIDS diagnosis, the development of vaccines, and screening for the hormone analogues, demonstrate just some of the possibilities that have been opened up by multiple peptide synthesis methods.</p>
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<abstract type="short" xml:lang="en"><p><b>Peptide fishing</b>
is a new sport in bioorganic and medicinal chemistry–biologically active peptides are identified from an ocean of peptides of various lengths and constitutions. In the last few years new methods have been developed for the synthesis of such peptide collections. Automation is the next step. For example, in immuno‐analysis the pin method is very important. Minute amounts of peptide are synthesized on rods (a few hundred simultaneously) and incubated with sera containing antibodies for the analysis. In this way the relevant epitopes, that is, the regions to which the antibodies bind, can be precisely determined and mapped.</p>
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<abstract lang="en">Rapid developments in the biotechnology of new proteins, as well as advances in immunology and the development of pharmaceuticals based on inhibitors and antagonists, have led to immense demands for synthetic peptides. Simultaneous preparation of 100–150 completely different peptides, having chain lengths of up to 20 amino acids can nowadays be achieved using multiple synthesis methods. The yields and qualities of the peptides so obtained are high enough to permit reliable in vivo and in vitro screening for biological activities. Moreover, it is possible to optimize synthetic conditions and to carry out comparative studies on the secondary structures and conformational mapping of proteins. Special multiple synthesis methods facilitate the epitope mapping of larger peptides for diagnostic purposes and for the development of vaccines based on a few hundreds of free or rod‐bound peptides that are useful for immunoassays. Multiple methods of peptide synthesis also enable the preparation of so‐called peptide libraries which could comprise hundreds of thousands of peptides, and by which new perspectives for the screening of lead structures will be opened up. Peptide synthesis using a combination of photolabile protecting groups and photolithographic procedures enables the assembling of peptide libraries on small plates for use in miniature immunoassays. Furthermore, lipopeptide‐antigen conjugates allow both the preparation of peptide‐specific and monoclonal antibodies as well as a complete screening of epitopes of B‐, T‐helper and T‐killer cells. Applications in the areas of AIDS diagnosis, the development of vaccines, and screening for the hormone analogues, demonstrate just some of the possibilities that have been opened up by multiple peptide synthesis methods.</abstract>
<abstract type="short" lang="en">Peptide fishing is a new sport in bioorganic and medicinal chemistry–biologically active peptides are identified from an ocean of peptides of various lengths and constitutions. In the last few years new methods have been developed for the synthesis of such peptide collections. Automation is the next step. For example, in immuno‐analysis the pin method is very important. Minute amounts of peptide are synthesized on rods (a few hundred simultaneously) and incubated with sera containing antibodies for the analysis. In this way the relevant epitopes, that is, the regions to which the antibodies bind, can be precisely determined and mapped.</abstract>
<note type="content">*Dedicated to Professor Ernst Bayer on the occasion of his 65th birthday</note>
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<name type="personal"><namePart type="given">G.</namePart>
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<place><placeTerm type="text">Berlin</placeTerm>
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<part><date>1989</date>
</part>
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<relatedItem type="references" displayLabel="cit2"><titleInfo><title>Peptides 1990, Proc. 21st Eur. Pept. Symp. (Eds.:E. Giralt,D. Andreu),Escom, Leiden,1991.</title>
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<note type="citation/reference">Peptides 1990, Proc. 21st Eur. Pept. Symp. (Eds.: E. Giralt, D. Andreu), Escom, Leiden, 1991.</note>
<name type="personal"><namePart type="given">E.</namePart>
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<part><date>1991</date>
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<relatedItem type="references" displayLabel="cit3"><titleInfo><title>Peptides: Chemistry and Biology, Proc. 10th Am. Pept. Symp. (Ed.:G. R. Marshall),Escom, Leiden,1988.</title>
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<name type="personal"><namePart type="given">G. R.</namePart>
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<relatedItem type="references" displayLabel="cit4"><titleInfo><title>(a)Peptides, Chemistry, Structure and Biology, Proc. 11th Am. Pept. Symp. (Eds.:J. E. Rivier,G. R. Marshall),Escom, Leiden,1990;</title>
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<note type="citation/reference">(a) Peptides, Chemistry, Structure and Biology, Proc. 11th Am. Pept. Symp. (Eds.: J. E. Rivier, G. R. Marshall), Escom, Leiden, 1990;</note>
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<note type="citation/reference">(b) Peptides, Chemistry and Biology Proc. 12th Am. Pept. Symp. (Eds.: J. A. Smith, J. E. Rivier), Escom, Leiden, 1992.</note>
<name type="personal"><namePart type="given">J. A.</namePart>
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<part><date>1992</date>
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</relatedItem>
<relatedItem type="references" displayLabel="cit6"><titleInfo><title>(a)Innovation and Perspectives in Solid Phase Synthesis: Peptides, Polypeptides and Oligonucleotides, Macro‐Organic Reagents and Catalysts–1990 (Ed.:R. Epton),SPCC, Birmingham,1990;</title>
</titleInfo>
<note type="citation/reference">(a) Innovation and Perspectives in Solid Phase Synthesis: Peptides, Polypeptides and Oligonucleotides, Macro‐Organic Reagents and Catalysts–1990 (Ed.: R. Epton), SPCC, Birmingham, 1990;</note>
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<titleInfo><title>(b)Innovation and Perspectives in Solid Phase Synthesis and Related Technologies: Peptides, Polypeptides and Oligonucleotides, 1991 (Ed.:R. Epton),Intercept, Andover,1992.</title>
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<relatedItem type="references" displayLabel="cit8"><titleInfo><title>(a)Peptide Chemistry 1987, Proc. 25th Symp. Pept. Chem. (Eds.:T. Shiba,S. Sakakibara),Protein Research Foundation, Osaka,1988;</title>
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<relatedItem type="references" displayLabel="cit10"><titleInfo><title>(a)Forum Peptides, Proc. 1st Int. Forum Pept. (Eds.:B. Castro,J. Martinez),Centre de Pharmacologie–Endocrinologie, Montpellier,1984;</title>
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