A new ligand for immunoglobulin G subdomains by screening of a synthetic peptide library (Articolo in rivista)

Type
Label
  • A new ligand for immunoglobulin G subdomains by screening of a synthetic peptide library (Articolo in rivista) (literal)
Anno
  • 2005-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1002/cbic.200400368 (literal)
Alternative label
  • Verdoliva, Antonio; Marasco, Daniela; De Capua, Antonia; Saporito, Angela; Bellofiore, Piero; Manfredi, Vincenzo; Fattorusso, Roberto; Pedone, Carlo; Ruvo, Menotti. (2005)
    A new ligand for immunoglobulin G subdomains by screening of a synthetic peptide library
    in ChemBioChem (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Verdoliva, Antonio; Marasco, Daniela; De Capua, Antonia; Saporito, Angela; Bellofiore, Piero; Manfredi, Vincenzo; Fattorusso, Roberto; Pedone, Carlo; Ruvo, Menotti. (literal)
Pagina inizio
  • 1242 (literal)
Pagina fine
  • 1253 (literal)
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  • 6 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#descrizioneSinteticaDelProdotto
  • Pubblicazione scientifica (literal)
Note
  • ISI Web of Science (WOS) (literal)
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  • Verdoliva, Bellofiore, Manfredi: Tecnogen SCPA Marasco, Ruvo, Pedone, Saporito De Capua: IBB, Istituto di Biostrutture e Bioimmagini del CNR Fattorussi: SUN (literal)
Titolo
  • A new ligand for immunoglobulin G subdomains by screening of a synthetic peptide library (literal)
Abstract
  • By screening a synthetic peptide library of general formula (NH2-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 IgG. The peptide, after a preliminary chromatog. characterization, has proved useful as a new affinity ligand for the purifn. of polyclonal as well as monoclonal antibodies from biol. fluids, with recovery yields of up to 90% (90% purity). The ligand is able to bind antibody fragments contg. 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 assocn. with the striking similarities of the peptide (named Fc-receptor mimetic, FcRM) with a region of the human Fcƒ×RIII 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 purifn. of antibody fragments and as a lead for the generation of Fc-receptor antagonists. (literal)
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