Binding properties of HABA-type azo derivatives to avidin and avidin-related protein 4

Susanna Repo, Tiina A.Paldanius [Unknown], Vesa P. Hytönen, Thomas Nyholm, Katrin K. Halling, Juhani Huuskonen, Olli T. Pentikäinen, Kari Rissanen, J Peter Slotte, Tomi Airenne, Tiina Salminen, Markku S .Kulomaa, Mark S Johnson

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36 Citations (Scopus)


The chicken genome encodes several biotin-binding proteins, including avidin and avidin-related protein 4 (AVR4). In addition to D-biotin, avidin binds an azo dye compound, 4-hydroxyazobenzene-2-carboxylic acid (HABA), but the HABA-binding properties of AVR4 are not yet known. Differential scanning calorimetry, UV/visible spectroscopy, and molecular modeling were used to analyze the binding of 15 azo molecules to avidin and AVR4. Significant differences are seen in azo compound preferences for the two proteins, emphasizing the importance of the loop between strands beta 3 and beta 4 for azo ligand recognition; information on these loops is provided by the high-resolution (1.5 angstrom) X-ray structure for avidin reported here. These results may be valuable in designing improved tools for avidin-based life science and nanobiotechnology applications.
Original languageUndefined/Unknown
Pages (from-to)1029–1039
Number of pages11
JournalChemistry and Biology
Issue number10
Publication statusPublished - 2006
MoE publication typeA1 Journal article-refereed

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