Selection of peptides inhibiting a ß-lactamase-like activity

Anne‐sophie Yribarren (1) , Daniel Thomas (1) , Alain Friboulet (1) , Bérangère Avalle (1)

1 GEC - Génie Enzymatique et Cellulaire

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.

Mots clés: catalytic antibodies; anti-idiotypy; β-lactamase; phage display library; constrained peptide

Domaines: Chimie

Anne‐sophie Yribarren, Daniel Thomas, Alain Friboulet, Bérangère Avalle. Selection of peptides inhibiting a ß-lactamase-like activity. European Journal of Biochemistry, 2003, 270 (13), pp.2789-2795. ⟨10.1046/j.1432-1033.2003.03651.x⟩. ⟨hal-00086183⟩