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

A1 Journal article (refereed)

Internal Authors/Editors

Publication Details

List of Authors: Susanna Repo, Tiina A.Paldanius, Vesa P. Hytönen, Thomas K. M. Nyholm, Katrin K. Halling, Juhani Huuskonen, Olli T. Pentikäinen, Kari Rissanen, J. Peter Slotte, Tomi T. Airenne, Tiina A. Salminen, Markku S .Kulomaa, Mark S.Johnson
Publisher: CELL PRESS
Publication year: 2006
Journal: Chemistry and Biology
Journal acronym: CHEM BIOL
Volume number: 13
Issue number: 10
Start page: 1029
End page: 1039
Number of pages: 11
ISSN: 1074-5521


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.

Last updated on 2020-08-04 at 04:32