Journal of Undergraduate Research


TNP fluorophore, adenosin binding, SNAP25B SNARE, binding protein


Life Sciences


Physiology and Developmental Biology


Vesicle fusion is a key step in the cellular process of exocytosis and is at the center of neurotransmitter release by neurons. Fusion is driven by a set of proteins known as SNAREs which includes the protein SNAP25B.

In the synthesis and spectroscopic analysis of the SNAP25B protein, a strong, unexpected 260 nm peak has been seen. This 260 nm peak might correspond to DNA, RNA, or any other adenosine-containing molecule binding to SNAP25B. Previous work indicated that the 260 peak was not due to DNA or RNA. SNAP25B binding to an adenosine-containing substance could be the basis of an important regulatory process in exocytosis. Knowing whether or not ATP, ADP, or AMP binds to SNAP25B may provide imperative insight into the true mechanism of exocytotic release.

The purpose of this project was to (1) identify whether or not ATP, ADP, or AMP bind to the SNAP25B protein, (2) determine the rate constants of binding, and (3) understand how this binding may affect SNAP25B conformation and its relationship to the formation of the SNARE complex for exocytosis.

Included in

Physiology Commons