Selection of peptides inhibiting a beta-lactamase-like activity
| Autor: | Anne-Sophie Yribarren, Daniel Thomas, Bérangère Avalle, Alain Friboulet |
|---|---|
| Rok vydání: | 2003 |
| Předmět: |
chemistry.chemical_classification
Phage display biology Active site Antibodies Catalytic Enzyme-Linked Immunosorbent Assay Peptide Surface Plasmon Resonance Biochemistry Molecular biology beta-Lactamases chemistry Peptide Library Immunoglobulin G biology.protein Animals Amino Acid Sequence Enzyme Inhibitors Surface plasmon resonance Antibody Peptides beta-Lactamase Inhibitors Protein Binding |
| Zdroj: | European Journal of Biochemistry. 270:2789-2795 |
| ISSN: | 1432-1033 0014-2956 |
| DOI: | 10.1046/j.1432-1033.2003.03651.x |
| Popis: | A library of random peptide sequences was used to select peptides that inhibit an anti-idiotypic catalytic Ig, immunoglobulin (IgG) 9G4H9, with a beta-lactamase-like activity. This library displays cyclic heptapeptides on the surface of bacteriophages and represents a collection of up to 4.5 x 109 peptides. The first selection step aimed at enriching the library in species that bind to the whole Ig molecule. The second step was to discriminate peptides that bind to part of the molecule other than the active site. Selected peptides were then screened by surface plasmon resonance analysis. Those displaying measurable Kd values were assayed for their ability to inhibit the catalytic Ig. |
| Databáze: | OpenAIRE |
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