TAILIEUCHUNG - Báo cáo khoa học: Selection of peptides inhibiting a b-lactamase-like activity

A library of random peptide sequences was used to select peptides that inhibit an anti-idiotypic catalytic Ig, immuno-globulin (IgG) 9G4H9, withab-lactamase-like activity. This library displays cyclic heptapeptides on the surface of bac-teriophagesand ·10 9 peptides. The first selection step aimed at enriching the lib-rary in species that bind to the whole Ig molecule. The sec-ond stepwas todiscriminate peptides that bind topart of the molecule other than the active site. Selected peptides were then screened by surface plasmon resonance analysis. Those displaying measurableKd values were assayed for their ability to inhibit the catalytic Ig | Eur. J. Biochem. 270 2789-2795 2003 FEBS 2003 doi Selection of peptides inhibiting a b-lactamase-like activity Anne-Sophie Yribarren Daniel Thomas Alain Friboulet and Berangere Avalle Genie enzymatique et cellulaire UMR 6022 CNRS Universite de Technologie de Compiegne France A library of random peptide sequences was used to select peptides that inhibit an anti-idiotypic catalytic Ig immunoglobulin IgG 9G4H9 with a b-lactamase-like activity. This library displays cyclic heptapeptides on the surface of bacteriophages and represents a collection of up to 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. Keywords catalytic antibodies anti-idiotypy b-lactamase phage display library constrained peptide. The elucidation of the rules governing the relationships between the structure of proteins and their function is currently one of the major challenges. In this field combinatorial approaches offer tremendous possibilities. The main requirement is to be able to sort from the engineered diversity mutants or new compounds according to the required function. Random peptide libraries are inexhaustible sources of small compounds likely to bind targets such as enzymes antibodies receptors or even DNA recently reviewed in 1 . Combinatorial libraries can be chemically synthesized or displayed on engineered bacteriophages as proposed by Smith s pioneer studies from the 1980s 2 3 . The use of phages allows one to workon huge libraries. It allows rapid isolation of the sequence of the selected compounds leading to the identification of residues involved in the interaction 4 . We have developed previously

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