Student Presenter(s): Jennifer Gattus
Faculty Mentor: Jole Fiorito
Department: Biological and Chemical Sciences
School/College: College of Arts and Sciences, Long Island

Alzheimer’s disease is a neurodegenerative disease that results in memory loss and reduction in cognitive function due to the accumulation of amyloid plaques and fibrillary tangles. According to the CDC, 5.8 million Americans lived with Alzheimer’s disease in 2020. Previous research has explored the relationship between modulating histone acetyltransferase (HAT) activity and improvement from defects in synaptic function and memory after amyloid plaque development. HAT enzymes add an acetyl group to lysine residues of histone proteins, regulating the expression of several memory-related genes during memory formation and/or consolidation. The HAT enzyme uses an acetyl group from acetyl-coA resulting in the production of the acetylated histone and free coenzyme A (CoA). The purpose of this study is to develop a fluorescence assay to detect any change of HAT enzyme p300 activity on histone 3.3 in the presence of HAT modulators. We use a fluorescent molecule, which binds to the sulfhydryl groups of CoA and generates a fluorescent signal. Our results so far have shown that the assay is working properly with significant differences between the substrate control (in the absence of p300) and positive control (in the presence of p300). Our experimental conditions have confirmed anacardic acid as an inhibitor (20% inhibition at 15µM) and YF2 as an activator (17% activation at 100nM). This enzymatic assay will be used for measuring the p300 activity of newly synthesized compounds.