A new ligand for immunoglobulin g subdomains by screening of a synthetic peptide library.
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| Abstract |
By screening a synthetic peptide library of general formula (NH(2)-Cys1-X2-X3-X4)(2)-Lys-Gly-OH, a disulfide-bridged cyclic peptide, where X2-X3-X4 is the tripeptide Phe-His-His, has been selected as a ligand for immunoglobulin G (IgG). The peptide, after a preliminary chromatographic characterization, has proved useful as a new affinity ligand for the purification of polyclonal as well as monoclonal antibodies from biological fluids, with recovery yields of up to 90% (90% purity). The ligand is able to bind antibody fragments containing both Fab and Fc from different antibody isotypes, a fact suggesting the presence of at least two different antibody-binding sites. While the recognition site on Fab is unknown, comparative binding studies with Fc, in association with the striking similarities of the peptide (named Fc-receptor mimetic, FcRM) with a region of the human FcgammaRIII receptor, strongly indicate that the peptide could recognize a short amino acid stretch of the lower hinge region, which has a key role in autoimmune disease triggering. The unique properties make the ligand attractive for both the purification of antibody fragments and as a lead for the generation of Fc-receptor antagonists.
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| Authors | Antonio Verdoliva, Daniela Marasco, Antonia De Capua, Angela Saporito, Piero Bellofiore, Vincenzo Manfredi, Roberto Fattorusso, Carlo Pedone, Menotti Ruvo |
| Journal | Chembiochem : a European journal of chemical biology (Chembiochem) Vol. 6 Issue 7 Pg. 1242-53 (Jul 2005) ISSN: 1439-4227 [Print] Germany |
| PMID | 15937987 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't) |
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