Multi-pin peptide synthesis strategy for T cell determinant analysis
Identifieur interne : 004A25 ( Main/Exploration ); précédent : 004A24; suivant : 004A26Multi-pin peptide synthesis strategy for T cell determinant analysis
Auteurs : N. Joe Maeji [Australie] ; Andrew M. Bray [Australie] ; H. Mario Geysen [Australie]Source :
- Journal of Immunological Methods [ 0022-1759 ] ; 1990.
English descriptors
- Teeft :
- Acetic acid, Amino, Amino acid, Amino acid analyses, Amino acid analysis, Amino acids, Antibody binding, Assay, Cell clone, Cell culture assays, Cell determinant, Cell determinant analysis, Cell determinant studies, Cell determinants, Cell epitopes, Cell proliferation, Chem, Cleavable, Cleavable linker, Cleavable linker group, Cleavage, Cleavage procedure, Cleavage rate, Cleavage solution, Commonwealth serum laboratories, Cyanogen bromide, Ddalinstkiysyfpsvi skvnqgaqgi, Deprotection, Determinant, Diketopiperazine, Diketopiperazine formation, Epitope, Fmoc group, Geysen, Good purity, Hplc, Hplc traces, Hydroxide, Intramolecular aminolysis, Ionic strength, Large numbers, Linker, Linker groups, Many peptides, Microtitre plates, Minimum reactive sequence, Nmol, Organic solvents, Peptide, Peptide cleavage, Peptide solutions, Peptide synthesis, Phosphate buffer, Polyethylene pins, Room temperature, Side chain deprotection, Side reaction, Simultaneous synthesis, Sodium hydroxide, Solid phase peptide synthesis, Terminal acetylated, Terminal moiety, Tetanus toxin, Trifluoroacetic acid, Tritiated thymidine, Waters associates.
Abstract
Abstract: Techniques to synthesize many peptides simultaneously exist, however their individual cleavage and subsequent purification constitutes a bottleneck to total throughput. Biological screening of peptides is generally carried out at physiological pH in aqueous solutions. However, peptides, unless individually purified are usually contaminated by residual compounds used in their preparation such as trifluoroacetic acid, organic solvents, scavengers etc. In testing with cellular systems, such as T cell determinant analysis, such contaminations must be rigorously excluded. We have extended the pin synthesis technique of synthesizing and screening large number of peptides (Geysen et al., 1984) to the analysis of T cell determinants. Peptides can be synthesized on polyethylene pins, the side chain protective groups removed and the peptides washed free of contaminants. A linker system stable under these conditions can then be triggered to cleave the peptides from the pins in an aqueous solution at neutral pH. This strategy enables the rapid mapping of T cell determinants. It is also applicable to other systems where large numbers of solution phase peptides are required, for example, in the study of hormone analogues.
Url:
DOI: 10.1016/0022-1759(90)90108-8
Affiliations:
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<term>Amino</term>
<term>Amino acid</term>
<term>Amino acid analyses</term>
<term>Amino acid analysis</term>
<term>Amino acids</term>
<term>Antibody binding</term>
<term>Assay</term>
<term>Cell clone</term>
<term>Cell culture assays</term>
<term>Cell determinant</term>
<term>Cell determinant analysis</term>
<term>Cell determinant studies</term>
<term>Cell determinants</term>
<term>Cell epitopes</term>
<term>Cell proliferation</term>
<term>Chem</term>
<term>Cleavable</term>
<term>Cleavable linker</term>
<term>Cleavable linker group</term>
<term>Cleavage</term>
<term>Cleavage procedure</term>
<term>Cleavage rate</term>
<term>Cleavage solution</term>
<term>Commonwealth serum laboratories</term>
<term>Cyanogen bromide</term>
<term>Ddalinstkiysyfpsvi skvnqgaqgi</term>
<term>Deprotection</term>
<term>Determinant</term>
<term>Diketopiperazine</term>
<term>Diketopiperazine formation</term>
<term>Epitope</term>
<term>Fmoc group</term>
<term>Geysen</term>
<term>Good purity</term>
<term>Hplc</term>
<term>Hplc traces</term>
<term>Hydroxide</term>
<term>Intramolecular aminolysis</term>
<term>Ionic strength</term>
<term>Large numbers</term>
<term>Linker</term>
<term>Linker groups</term>
<term>Many peptides</term>
<term>Microtitre plates</term>
<term>Minimum reactive sequence</term>
<term>Nmol</term>
<term>Organic solvents</term>
<term>Peptide</term>
<term>Peptide cleavage</term>
<term>Peptide solutions</term>
<term>Peptide synthesis</term>
<term>Phosphate buffer</term>
<term>Polyethylene pins</term>
<term>Room temperature</term>
<term>Side chain deprotection</term>
<term>Side reaction</term>
<term>Simultaneous synthesis</term>
<term>Sodium hydroxide</term>
<term>Solid phase peptide synthesis</term>
<term>Terminal acetylated</term>
<term>Terminal moiety</term>
<term>Tetanus toxin</term>
<term>Trifluoroacetic acid</term>
<term>Tritiated thymidine</term>
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<front><div type="abstract" xml:lang="en">Abstract: Techniques to synthesize many peptides simultaneously exist, however their individual cleavage and subsequent purification constitutes a bottleneck to total throughput. Biological screening of peptides is generally carried out at physiological pH in aqueous solutions. However, peptides, unless individually purified are usually contaminated by residual compounds used in their preparation such as trifluoroacetic acid, organic solvents, scavengers etc. In testing with cellular systems, such as T cell determinant analysis, such contaminations must be rigorously excluded. We have extended the pin synthesis technique of synthesizing and screening large number of peptides (Geysen et al., 1984) to the analysis of T cell determinants. Peptides can be synthesized on polyethylene pins, the side chain protective groups removed and the peptides washed free of contaminants. A linker system stable under these conditions can then be triggered to cleave the peptides from the pins in an aqueous solution at neutral pH. This strategy enables the rapid mapping of T cell determinants. It is also applicable to other systems where large numbers of solution phase peptides are required, for example, in the study of hormone analogues.</div>
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