Epitope mapping of the monoclonal antibody MM12.10 to external MDR1 P-glycoprotein domain by synthetic peptide scanning and phage display technologies

Romagnoli, G.; Poloni, F.; Flego, M.; Moretti, F.; Di Modugno, F.; Chersi, A.; Falasca, G.; Signoretti, C.; Castagna, M.; Cianfriglia, M.

Biological Chemistry 380(5): 553-559

1999


ISSN/ISBN: 1431-6730
PMID: 10384961
DOI: 10.1515/bc.1999.070
Accession: 010599931

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Abstract
Epitope mapping of MDR1-P-glycoprotein using specific monoclonal antibodies (mAbs) may help in delineating P-glycoprotein topology and hence in elucidating the relationship between its structural organization and drug-efflux pump function. In this work, by using synthetic peptide scanning and phage display technologies, the binding sites of the mAb MM12.10, a novel antibody to intact human multidrug resistant (MDR) cells, were studied. The results we obtained confirm that two regions localized on the predicted fourth and sixth loops are indeed external and that MDR1 peptides covering the inner domain of the current 12 transmembrane segment (TMs) model of P-glycoprotein could form part of the MM12.10 epitope.