Open AccessSelection of peptides inhibiting a β‐lactamase‐like activity
Author(s) -
Yribarren AnneSophie,
Thomas Daniel,
Friboulet Alain,
Avalle Bérangère
Publication year - 2003
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1046/j.1432-1033.2003.03651.x
Subject(s) - surface plasmon resonance , peptide , peptide library , chemistry , selection (genetic algorithm) , antibody , phage display , combinatorial chemistry , biochemistry , computational biology , stereochemistry , microbiology and biotechnology , peptide sequence , biology , gene , nanotechnology , genetics , computer science , materials science , artificial intelligence , nanoparticle
A library of random peptide sequences was used to select peptides that inhibit an anti‐idiotypic catalytic Ig, immunoglobulin (IgG) 9G4H9, with a β‐lactamase‐like activity. This library displays cyclic heptapeptides on the surface of bacteriophages and represents a collection of up to 4.5 × 10 9 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 K d values were assayed for their ability to inhibit the catalytic Ig.