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Titolo:
DiSSiMiL: Diverse Small Size Mini-Libraries applied to simple and rapid epitope mapping of a monoclonal antibody
Autore:
Burgess, K; Han, I; Zhang, A; Zheng, WH; Shanmugam, K; Featherstone, MS; Saragovi, HU;
Indirizzi:
McGill Univ, Dept Pharmacol & Therapeut, Montreal, PQ H3G 1Y6, Canada McGill Univ Montreal PQ Canada H3G 1Y6 peut, Montreal, PQ H3G 1Y6, Canada Texas A&M Univ, Dept Chem, College Stn, TX 77843 USA Texas A&M Univ College Stn TX USA 77843 t Chem, College Stn, TX 77843 USA McGill Univ, Dept Oncol, Montreal, PQ, Canada McGill Univ Montreal PQ Canada ll Univ, Dept Oncol, Montreal, PQ, Canada McGill Univ, Ctr Canc, Montreal, PQ, Canada McGill Univ Montreal PQ Canada Gill Univ, Ctr Canc, Montreal, PQ, Canada
Titolo Testata:
JOURNAL OF PEPTIDE RESEARCH
fascicolo: 1, volume: 57, anno: 2001,
pagine: 68 - 76
SICI:
1397-002X(200101)57:1<68:DDSSMA>2.0.ZU;2-D
Fonte:
ISI
Lingua:
ENG
Soggetto:
SYNTHETIC COMBINATORIAL LIBRARIES; SOLID-PHASE SYNTHESIS; NERVE GROWTH-FACTOR; THERMODYNAMIC CHARACTERIZATION; COOPERATIVE INTERACTIONS; PEPTIDE AGONIST; BINDING DOMAIN; PHAGE DISPLAY; AMINO-ACIDS; ANTIGEN;
Keywords:
binding; drug discovery; epitope mapping; peptide library;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
42
Recensione:
Indirizzi per estratti:
Indirizzo: Saragovi, HU McGill Univ, Dept Pharmacol & Therapeut, 3655 Drummond St,1320, Montreal, PQ H3G 1Y6, Canada McGill Univ 3655 Drummond St,1320 Montreal PQ Canada H3G 1Y6
Citazione:
K. Burgess et al., "DiSSiMiL: Diverse Small Size Mini-Libraries applied to simple and rapid epitope mapping of a monoclonal antibody", J PEPT RES, 57(1), 2001, pp. 68-76

Abstract

Methods for screening protein-protein interactions are useful in protein science and for the generation of drug leads. We set out to develop a simplified assay to rapidly test protein-protein interactions, with a library of 400 pentapeptides comprising the 20 natural amino acids at two variable positions followed by three glycines (NH2-X(1)X(2)GGG). The library was used to identify the epitope of monoclonal antibody (mAb) 10D11 directed against the HOXD4 protein. Three pentapeptide 'hits' were selected (VYGGG, PWGGG and WKGGG) from direct binding assays screening for pentapeptide mAb interactions; and from assays using pentapeptides in solution to competitively block HOXD4 mAb interactions. Alignment of the three 'hit' pentapeptides to theHOXD4 sequence predicts the mAb 10D11 epitope as NH2-VYPWMK. Synthesis of NH2-VYPWMK hexapeptide confirmed this prediction; and an alanine scan of HOXD4 ablated binding by mAb 10D11 when amino acids in the putative epitope were mutated. We propose that these simplified hut diverse libraries can be used for rapid epitope mapping of some mAbs, and for generating lead small peptide analogs that interfere with receptor-ligand or other protein-protein interactions, or with enzymatic activity.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/04/20 alle ore 02:15:09