Alea Sterling


Alea Sterling





Alea is from Fort-Lauderdale, Florida. She is currently majoring in health science: Pre-clinical. Her research involves the observation of Neurotoxicity of Alzheimer's Amyloid-Beta via analyzing the conformational changes of Amyloid-Beta peptide. This research will elucidate the onset of Alzheimer’s and contribute to treatment medication. The brain is one of the most complex and misunderstood structure of the body. I plan to pursue a career in neuroscience where I can contribute to neurological education.

Faculty Mentor

Suren Tatulian, Ph.D.

Undergraduate Major

Health Science Pre-clinical

Future Plans

Neuroscience PhD/ Neurologist MD


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

Mentor: Suren, Tatulian Ph.D

Abstract: Alzheimer’s disease (AD) is neurogenerative disorder commonly associated with age- related dementia and is characterized by the accumulation of amyloid precursors in the brain. Amyloid beta (AB) peptide is an important factor in analyzing the onset of the Alzheimer’s Disease and is present in several forms. These oligomeric precursors interact with the neuronal membrane exerting several neurotoxic mechanisms: 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; however, the underlying contribution in the initiation and progression of AD remains unknown. The objective of this project is to analyze the relationship between the aggregation and structural state of AB peptide and its neurotoxic properties by observing its conformational changes over time. To accomplish this, peptide, AB 25-35, will be suspended in an aqueous buffer that mimics extracellular fluids in the brain. Thioflavin T Fluoresence (ThT) was used to monitor the time course of aggregation of the peptide, and circular dichroism spectroscopy was used to record the conformational changes. The results are expected to provide a thorough explanation of the mechanism underlying the toxicity of AB formation and the structural details of peptide aggregation.


Medicine and Health Sciences

Alea Sterling