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Titolo:
Generation and refinement of peptide mimetic ligands for paratope-specificpurification of monoclonal antibodies
Autore:
Murray, A; Smith, RG; Brady, K; Williams, S; Badley, RA; Price, MR;
Indirizzi:
Univ Nottingham, Sch Pharmaceut Sci, Canc Res Labs, Nottingham NG7 2RD, England Univ Nottingham Nottingham England NG7 2RD , Nottingham NG7 2RD, England Unilever Res Labs, Colworth Lab, Biorecognit Unit, Sharnbrook MK44 1LQ, Beds, England Unilever Res Labs Sharnbrook Beds England MK44 1LQ K44 1LQ, Beds, England
Titolo Testata:
ANALYTICAL BIOCHEMISTRY
fascicolo: 1, volume: 296, anno: 2001,
pagine: 9 - 17
SICI:
0003-2697(20010901)296:1<9:GAROPM>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
EPITOPE AFFINITY-CHROMATOGRAPHY; PHAGE-DISPLAY; FINE SPECIFICITY; PROTEIN CORE; MIMOTOPES; LIBRARY; IDENTIFICATION; CARCINOMAS; DISCOVERY; FRAGMENT;
Keywords:
affinity chromatography; mimotope; monoclonal antibody; replacement net analysis; phage display;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
35
Recensione:
Indirizzi per estratti:
Indirizzo: Murray, A Univ Nottingham, Sch Pharmaceut Sci, Canc Res Labs, Nottingham NG7 2RD, England Univ Nottingham Nottingham England NG7 2RD am NG7 2RD, England
Citazione:
A. Murray et al., "Generation and refinement of peptide mimetic ligands for paratope-specificpurification of monoclonal antibodies", ANALYT BIOC, 296(1), 2001, pp. 9-17

Abstract

Paratope-specific purification of antibodies has distinct advantages over conventional methods of antibody purification with respect to its capacity to isolate product of high purity and immunoreactivity. The present report addresses the problems of identifying peptide ligands for the purification of antibodies reactive with nonprotein antigens. Using an anti-steroid antibody as the model, a lead sequence that bound antibody was identified from a peptide phage display library. The minimum binding unit in this sequence was deduced using a series of truncated peptides synthesized on the heads of polyethylene pins. Replacement Net analysis of the minimum binding unit identified peptides with increased affinity for the antibody. The affinity-matured peptide mimotope bound antibody in solution. By molecular modeling the peptide was superimposable onto estrone-3-glucuronide localized in the crystal structure of the antibody binding pocket. In order to resolve problems of presentation posed by the reversal of orientation of the peptide on the affinity matrix compared with the pins, the mimotope peptide was synthesized in reverse sequence using D-amino acids. The resulting affinity matrixwas effective for the purification of antibody. Eluted product demonstrated molecular homogeneity and high immunoreactivity. It is concluded that thecombination of biological and chemical library techniques described provides a method for the generation and affinity maturation of mimotopes for antibodies against nonprotein antigens. (C) 2001 Academic Press.

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Documento generato il 27/09/20 alle ore 06:35:20