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Our research emphasis pertains to natural toxins
which interact specifically with receptor Site 1 (saxitoxin and
tetrodotoxin), Site 2 (batrachotoxin, veratridine, and aconitine),
and Site 5 (brevetoxins and ciguatoxin) associated with voltage-sensitive
sodium channels. Our current molecular pharmacology work requires
derivatization of each of these classes of toxin for use in biochemical
investigations of the binding phenomena. Computer modeling of proposed
derivatives, including structure-function relationships between
receptor and toxin ligand, aids in our efforts to describe the 3-dimensional
characteristics of each toxin binding site. A second avenue of research
pertains to the development of specific binding assays for marine
seafood toxins, with the express end product being colorometric
detection kits for public health use. Current work centers on preparing
immunological reagents for assay development, with future aspects
involving the specific membrane-bound toxin receptor in in vitro
microtitre plate formats and biosensor technology.
Baden, D.G., K.S. Rein, R.E. Gawley, G. Jeglitsch, and D.J. Adams.
1994. Is the a-ring lactone of brevetoxin PbTx-3 required for sodium
channel orphan receptor binding and activity. Natural Toxins 2:
212-221. [Winner of Quintessence award 1994]
Poli, M.A., K.S. Rein, and D.G. Baden. 1995. Radioimmunoassay for
the PbTx-2-type brevetoxins: eptiope specificity of two anti-PbTx
sera. J. Assoc. Official Analyt. Chem. Intl. 78: 538-542.
Trainer, V.L., D.G. Baden, and W.A. Catterall. 1995. Detection
of marine toxins using reconstituted sodium channels. J. Assoc.
Official Analyt. Chem. Intl. 78: 499-508.
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