Often calcium signaling is oscillatory, such as in the role it plays in triggering the enzyme calmodulin-dependent protein kinase II. A photochromic compound has been constructed which exists in open and closed form with a difference in binding affinity of about 100 fold.   A variety of modifications to the photochromic scaffold are hypothesized to improve the binding affinity for calcium. These include altering the structure of the aminocarboxylate ligand as well as the phenyl substituents on the naphthopyran ring system. The synthesis and characterization of model open and closed forms will be presented.   N-benzyl-N, N', N'-tris (tert-butyloxycarbonylmethyl) ethylenediamine was synthesized with purified yields of 81.14%, 66.55% and 30.3%.  Progress towards the synthesis of the target modified naphthopyran chelator also will be presented.

Developing chemical tools to help understand oscillatory calcium signaling

241st National Meeting (2011)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.