TAILIEUCHUNG - Báo cáo khoa học: Regional and segmental flexibility of antibodies in interaction with antigens of different size

The interaction of antibodies (Abs) with protein antigens (Ags) of different size, such as hen egg white lysozyme, ovalbumin, and bovine serum albu-min, was examined using analytical ultracentrifugation, electrospray ioniza-tion time-of-flight mass spectrometry, and surface plasmon resonance in order to estimate regional and segmental Ab flexibility. | iFEBS Journal Regional and segmental flexibility of antibodies in interaction with antigens of different size Masayuki Oda1 Susumu Uchiyama2 Carol V. Robinson3 Kiichi Fukui2 Yuji Kobayashi4 and Takachika Azuma5 1 Graduate Schoolof Agriculture Kyoto PrefecturalUniversity Japan 2 Graduate Schoolof Engineering Osaka University Japan 3 Department of Chemistry University of Cambridge UK 4 Graduate Schoolof PharmaceuticalSciences Osaka University Japan 5 Research Institute for BiologicalSciences RIBS Tokyo University of Science Chiba Japan Keywords antigen-antibody interaction analytical ultracentrifugation electrospray ionization time-of-flight mass spectrometry protein flexibility surface plasmon resonance Correspondence T. Azuma Research Institute for Biological Sciences RIBS Tokyo University of Science 2669 Yamazaki Noda Chiba 278-0022 Japan Fax 81 4 7121 4089 Tel 81 4 7121 4082 E-mail tazuma@ Received 29 November 2005 accepted 6 February 2006 doi The interaction of antibodies Abs with protein antigens Ags of different size such as hen egg white lysozyme ovalbumin and bovine serum albumin was examined using analytical ultracentrifugation electrospray ionization time-of-flight mass spectrometry and surface plasmon resonance in order to estimate regional and segmental Ab flexibility. When both Abs and Ags were free in solution sedimentation equilibrium and surface plasmon resonance analyses showed the formation of an Ag2Ab1 complexes regardless of Ag size suggesting that the Fab arms were able to move to avoid interference between Ags bound to Ab combining sites. The Ag2Ab1 complex as well as the Ag1Ab1 complex was observed by MS. However when Abs were immobilized on the surface of a sensor chip through the Fc region the stoichiometry of the Ag-Ab complex was dependent on the Ag size Ag2Ab1 forming with hen egg white lysozyme and Ag1Ab1 with ovalbumin and bovine serum albumin. These results indicated that immobilization

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