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

A1 Originalartikel i en vetenskaplig tidskrift (referentgranskad)

Interna författare/redaktörer

Publikationens författare: 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
Förläggare: CELL PRESS
Publiceringsår: 2006
Tidskrift: Chemistry and Biology
Tidskriftsakronym: CHEM BIOL
Volym: 13
Nummer: 10
Artikelns första sida, sidnummer: 1029
Artikelns sista sida, sidnummer: 1039
Antal sidor: 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.

Senast uppdaterad 2020-03-04 vid 07:15