Affinity capillary electrophoresis investigation of an epitope on human immunodeficiency virus recognized by a monoclonal antibody

Electrophoresis
X H Qian, K B Tomer

Abstract

Affinity capillary electrophoresis (ACE) has been used to investigate the epitope on the human immunodeficiency virus (HIV) core protein p24 recognized by the monoclonal antibody (mAb) 13-102-100. The affinity of a series of peptides with N- and C-terminal truncations of the epitope sequence determined by mass spectrometry was studied. The peak area change assay was used for the study of the interactions of the mAb with those peptides, exhibiting tight binding to the mAb, and the migration time shift assay was used to probe the relative affinities of peptides showing weak binding to the mAb. The experimental results show that the monoclonal antibody 13-102-100 recognizes the peptide VHPVHAGPIAP with highest affinity. Smaller peptides incorporating only part of the epitope, however, are recognized to some extent in the ACE experiments.

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Citations

Feb 21, 2007·Analytical and Bioanalytical Chemistry·Li-Wei ZhangXin-Xiang Zhang
Dec 7, 2007·Biotechnology & Genetic Engineering Reviews·Robert C Ladner
Apr 10, 2009·Journal of Molecular Biology·Eric BarklisClaudia S López
Jun 12, 2009·Electrophoresis·Niels H H Heegaard
Jun 23, 2007·Biomedical Chromatography : BMC·Suresh C V BabuYoung Sook Yoo
May 30, 2006·Electrophoresis·Jesper Ostergaard, Niels H H Heegaard
Feb 24, 2001·Electrophoresis·R M Guijt-van DuijnE Baltussen

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