Research Symposium

BIO

I am a biomedical engineering student at Florida State University with a strong passion for medicine, research, and patient care. As a pre-med student, I am dedicated to understanding the complexities of healthcare and exploring different medical specialties.

I am currently conducting research with the Mysona Group, focusing on protein molecular simulations to deepen my understanding of molecular interactions and their applications in biomedical science. My academic journey is driven by curiosity, problem-solving, and a commitment to contributing to advancements in medicine and healthcare technology.

With a strong foundation in science and engineering, I enjoy applying analytical thinking to real-world challenges. I am committed to continuous learning, personal growth, and making a meaningful impact in the medical field.

Prion Misfolding: Beta-Sheet Destabilization

Abstract

Prion diseases are a group of fatal neurodegenerative disorders caused by the misfolding of the prion
protein (PrP). The misfolded form propagates by converting native PrP into its pathogenic
conformation, yet the precise molecular mechanisms underlying this process remain poorly
understood. A key step in misfolding involves structural destabilization, particularly in the β-sheet
regions of PrP. Molecular dynamics (MD) simulations provide atomic-level insights into protein
misfolding, but conventional approaches are hindered by the large disparity between biologically
relevant folding timescales and computational limitations. To overcome this barrier, we employ
advanced sampling techniques to investigate the unzipping of the β-sheet in properly folded PrP, a
potential early-stage event in misfolding. Our simulations capture conformational transitions that
reveal key intermediates and energy barriers associated with β-sheet destabilization. By characterizing
these molecular events, we provide novel insight into the earliest structural changes that may lead to
prion propagation. Understanding these misfolding pathways is essential for elucidating prion disease
mechanisms and could inform future therapeutic strategies aimed at stabilizing the native PrP
conformation, thereby preventing disease onset.c

Keywords: Prion, Beta Sheet, Proteins