Insights on the amino acid side-chain interactions of a synthetic T-cell determinant
Autor: | Isidro Prieto, J. J. Golvano, Juan José Lasarte, A. Szabo, Pablo Sarobe, Francisco Borrás-Cuesta, J.G. Guillet, J.L. Guillaume |
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Rok vydání: | 1991 |
Předmět: |
Stereochemistry
medicine.drug_class T-Lymphocytes Molecular Sequence Data Bioengineering Peptide Monoclonal antibody Lymphocyte Activation Applied Microbiology and Biotechnology Epitopes/chemistry Epitope Cell Line Epitopes Structure-Activity Relationship Viral Proteins medicine Animals Viral Regulatory and Accessory Proteins Amino Acid Sequence Peptide sequence Pharmacology chemistry.chemical_classification Hybridomas General Immunology and Microbiology biology Edman degradation Antibodies Monoclonal General Medicine T-Lymphocytes/immunology Amino acid DNA-Binding Proteins Repressor Proteins S-tag Biochemistry chemistry Peptides/immunology biology.protein Antibody Peptides Biotechnology |
Zdroj: | Dadun. Depósito Académico Digital de la Universidad de Navarra instname |
ISSN: | 1045-1056 |
Popis: | The effect of single amino acid substitutions at positions 18 and 20 on the T-cell determinant (TD) character of peptide p12–26 from lambda repressor protein and on its recognition by a monoclonal antibody was studied by means of 40 synthetic peptides of a length of 15 amino acids. ELISA competition experiments showed that the identity of amino acid at position 20 is very important for antibody recognition, whereas that of amino acid at position 18 is much less important. In contrast, both Leu 18 and Ala 20 are important residues in defining the TD character of peptide p12–26. The most tolerated replacements, ordered in increasing disrupting power are: Ala 20 by Cys, Ser or Gly and Leu 18 by Ile or Val. Any other amino acid replacement completely abolishes the TD capacity of peptide p12–26. The peptides used in this study were synthesized using a multiple solid-phase peptide synthesizer newly designed. Their purity was very high as shown by amino acid sequence experiments. |
Databáze: | OpenAIRE |
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