Alea Sterling


Alea Sterling





Alea is from Fort-Lauderdale, Florida and is a Senior at the University of Central Florida. She is currently majoring in health science: Pre-clinical. Her research involves analyzing the relationship between the aggregation and structure of Amyloid-Beta peptide. This research will elucidate the onset of Alzheimer’s and contribute to possible treatment. By providing a structural mechanism of formation of these highly cytotoxic aggregation, we will be able to better understand its behavior. Alea plans to pursue a career in Dentistry where she would later specialize to be an Oral Surgeon.

Faculty Mentor

Suren Tatulian, Ph.D.

Undergraduate Major

Health Science Pre-clinical

Future Plans

Oral Maxillofacial Surgeon


Title: Aggregation and Structure of a Cytotoxic Fragment of Amyloid Beta Peptide.

Mentor: Suren, Tatulian Ph.D

Abstract: Alzheimer’s disease (AD) is a neurodegenerative disorder that constitutes the majority of cases of age-related dementia and is characterized by the accumulation of the amyloid beta (Ab) peptide aggregates in the brain. Ab peptide is involved in the onset and progression of AD and is present in several forms. The most abundant for of Ab is the 40 amino acid residue peptide (Ab1-40), but other forms, such as Ab1-42 and Ab25-35, exert stronger cytotoxic effect on neuronal cells by various mechanisms. Some of the established mechanisms of Ab cytotoxicity are membrane permeabilization, abnormal receptor activation, oxidative stress, and tau protein hyperphosphorylation. This disturbance in the balance of the neurological environment causes synaptic dysfunction, a common indicator of AD. There is strong experimental evidence indicating that the aggregation state and the structure of Ab assemblies play an essential role in toxicity. The objective of this project is to analyze the relationship between the aggregation and structure of Ab25-35 peptide. To accomplish this, Ab25-35 was suspended in an aqueous buffer containing thioflavin-T (ThT), a fluorophore that undergoes strong increase in fluorescence upon binding to Ab fibrils. ThT fluorescence was used to monitor the time course of aggregation of the peptide, and parallel circular dichroism measurements were used to record the conformational changes. The correlation between the aggregation state and structure of Ab25-35 is expected to provide a structural mechanism of formation of highly cytotoxic assemblies of the Ab25-35 peptide.


Medicine and Health Sciences

Alea Sterling