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

doi:10.1016/j.chembiol.2006.08.006

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

Research output: Contribution to journal › Article › Scientific › peer-review

38 Citations (Scopus)

Abstract

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 language	Undefined/Unknown
Pages (from-to)	1029–1039
Number of pages	11
Journal	Chemistry and Biology
Volume	13
Issue number	10
DOIs	https://doi.org/10.1016/j.chembiol.2006.08.006
Publication status	Published - 2006
MoE publication type	A1 Journal article-refereed

Access to Document

10.1016/j.chembiol.2006.08.006

https://www.sciencedirect.com/science/article/pii/S1074552106002973

Cite this

Repo, S., [Unknown], T. A. P., Hytönen, V. P., Nyholm, T., Halling, K. K., Huuskonen, J., Pentikäinen, O. T., Rissanen, K., Slotte, J. P., Airenne, T., Salminen, T., .Kulomaa, M. S., & Johnson, M. S. (2006). Binding properties of HABA-type azo derivatives to avidin and avidin-related protein 4. Chemistry and Biology, 13(10), 1029–1039. https://doi.org/10.1016/j.chembiol.2006.08.006

@article{87f4241d75a64bdf94c1b5ffaf1dc991,

title = "Binding properties of HABA-type azo derivatives to avidin and avidin-related protein 4",

abstract = "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.",

author = "Susanna Repo and [Unknown], {Tiina A.Paldanius} and Hyt{\"o}nen, {Vesa P.} and Thomas Nyholm and Halling, {Katrin K.} and Juhani Huuskonen and Pentik{\"a}inen, {Olli T.} and Kari Rissanen and Slotte, {J Peter} and Tomi Airenne and Tiina Salminen and .Kulomaa, {Markku S} and Johnson, {Mark S}",

year = "2006",

doi = "10.1016/j.chembiol.2006.08.006",

language = "Odefinierat/ok{\"a}nt",

volume = "13",

pages = "1029–1039",

journal = "Chemistry and Biology",

issn = "1074-5521",

number = "10",

}

Repo, S, [Unknown], TAP, Hytönen, VP, Nyholm, T, Halling, KK, Huuskonen, J, Pentikäinen, OT, Rissanen, K, Slotte, JP, Airenne, T , Salminen, T, .Kulomaa, MS & Johnson, MS 2006, 'Binding properties of HABA-type azo derivatives to avidin and avidin-related protein 4', Chemistry and Biology, vol. 13, no. 10, pp. 1029–1039. https://doi.org/10.1016/j.chembiol.2006.08.006

TY - JOUR

T1 - Binding properties of HABA-type azo derivatives to avidin and avidin-related protein 4

AU - Repo, Susanna

AU - [Unknown], Tiina A.Paldanius

AU - Hytönen, Vesa P.

AU - Nyholm, Thomas

AU - Halling, Katrin K.

AU - Huuskonen, Juhani

AU - Pentikäinen, Olli T.

AU - Rissanen, Kari

AU - Slotte, J Peter

AU - Airenne, Tomi

AU - Salminen, Tiina

AU - .Kulomaa, Markku S

AU - Johnson, Mark S

PY - 2006

Y1 - 2006

N2 - 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.

AB - 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.

U2 - 10.1016/j.chembiol.2006.08.006

DO - 10.1016/j.chembiol.2006.08.006

M3 - Artikel

SN - 1074-5521

VL - 13

SP - 1029

EP - 1039

JO - Chemistry and Biology

JF - Chemistry and Biology

IS - 10

ER -