Abstract

) Estrogen mimics are among the xenobiotics found to cause reproductive impairment and cancer long after they have been released in the environment. The wide variety of compounds, which potentially can act as hormone mimics, precludes any detection strategies based on structure, and there are no analytical tools capable of detecting these compounds to date. We therefore propose to develop a rapid, nanobalance quartz crystal system to monitor estrogenic substances in the environment. Our goal is to attach the hormone-binding domain of the estrogen receptor to a piezoelectric crystal and determine its potential as a sensor for estrogenic substances. This application offers the development of a new biological analytic technique that could monitor estrogenic substances both in the environment and in food products.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Cancer Institute (NCI)
Type
Small Research Grants (R03)
Project #
1R03CA089705-01
Application #
6286488
Study Section
Special Emphasis Panel (ZCA1-SRRB-7 (O1))
Program Officer
Malone, Winfred F
Project Start
2001-04-01
Project End
2003-03-31
Budget Start
2001-04-01
Budget End
2002-03-31
Support Year
1
Fiscal Year
2001
Total Cost
$74,618
Indirect Cost

  Institution

Name
Clarkson University
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
041590993
City
Potsdam
State
NY
Country
United States
Zip Code
13699

  Publications

Baltus, Ruth E; Carmon, Kendra S; Luck, Linda A (2007) Quartz crystal microbalance (QCM) with immobilized protein receptors: comparison of response to ligand binding for direct protein immobilization and protein attachment via disulfide linker. Langmuir 23:3880-5
Carmon, Kendra S; Baltus, Ruth E; Luck, Linda A (2005) A biosensor for estrogenic substances using the quartz crystal microbalance. Anal Biochem 345:277-83
Carmon, Kendra S; Baltus, Ruth E; Luck, Linda A (2004) A piezoelectric quartz crystal biosensor: the use of two single cysteine mutants of the periplasmic Escherichia coli glucose/galactose receptor as target proteins for the detection of glucose. Biochemistry 43:14249-56
Magnusson, Ulrika; Salopek-Sondi, Branka; Luck, Linda A et al. (2004) X-ray structures of the leucine-binding protein illustrate conformational changes and the basis of ligand specificity. J Biol Chem 279:8747-52
Salopek-Sondi, Branka; Skeels, Matthew C; Swartz, Derrick et al. (2003) Insight into the stability of the hydrophobic binding proteins of Escherichia coli: assessing the proteins for use as biosensors. Proteins 53:273-81
Salopek-Sondi, Branka; Vaughan, Mark D; Skeels, Matthew C et al. (2003) (19)F NMR studies of the leucine-isoleucine-valine binding protein: evidence that a closed conformation exists in solution. J Biomol Struct Dyn 21:235-46
Luck, Linda A; Moravan, Michael J; Garland, John E et al. (2003) Chemisorptions of bacterial receptors for hydrophobic amino acids and sugars on gold for biosensor applications: a surface plasmon resonance study of genetically engineered proteins. Biosens Bioelectron 19:249-59