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Studies on enantioselectivities of avidin, avidin-biotin complex and streptavidin by affinity capillary electrophoresis

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Summary

Various enantiomer separations were performed by affinity capillary electrophoresis with a partial filling technique (PFACE) using egg white avidin (AVI) and two avidin analogues: succinylated avidin (Suc-AVI) and streptavidin (STAV). Basic AVI was useful for enantiomer separation of acidic racemates, while the chemical modified acidic Suc-AVI was useful for that of basic racemates. Such a chemical modification of protein was effective in extending the applicability of the chiral selector in PFACE. STAV, which was a neutral nonglycosylated protein, was useful for both acidic and basic enantiomer separations. Although AVI and AVI analogues show similar biotin-binding activities, enantioselectivity was different among the proteins in this study. Additionally, we investigated whether the enantioselectivity was due to interaction of enantiomers with biotin-binding sites or not. Not only enantioselevtivity but also interaction with enantiomers was entirely lost by the formation of AVI-biotin complex.

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Authors and Affiliations

  1. Department of Analytical Chemistry, Nippon Boehringer Ingelheim Co. Ltd., 3-10-1, Yato, Kawanishi, 666-0193, Hyogo, Japan

    Y. Tanaka

  2. Department of Material Science, Faculty of Science, Himeji Institute of Technology, Kamigori, 678-1297, Hyogo, Japan

    S. Terabe

Authors
  1. Y. Tanaka
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  2. S. Terabe
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Tanaka, Y., Terabe, S. Studies on enantioselectivities of avidin, avidin-biotin complex and streptavidin by affinity capillary electrophoresis. Chromatographia 49, 489–495 (1999). https://doi.org/10.1007/BF02467747

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  • DOI: https://doi.org/10.1007/BF02467747

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