Organic Biochemistry Laboratory
Research Field
Dr. Ling-Hsien Tu is currently a Professor in the Department of Chemistry at National Taiwan Normal University, a position she has held since August 2024. Dr. Tu’s academic journey began with her Ph.D. in Chemistry, which she earned from Stony Brook University, New York, in August 2014. Her doctoral research focused on "Formation and Inhibition of Islet Amyloid in Type 2 Diabetes", under the guidance of Dr. Daniel P. Raleigh. Before joining National Taiwan Normal University, Dr. Tu gained valuable postdoctoral experience at the Genomics Research Center, Academia Sinica. She was a Distinguished Postdoctoral Scholar starting in January 2015. Dr. Tu’s research interests primarily revolve around amyloid formation, a complex process involving the polymerization of monomeric peptides or proteins into unbranched fibrils. Her work extends beyond understanding the underlying mechanisms of amyloid formation to developing therapeutic strategies. These strategies include the use of natural compounds, polymers, and nanomaterials to prevent amyloid formation. Additionally, her research group is actively engaged in identifying fluorescent molecules that can effectively distinguish different aggregated states.
My research interests mainly focus on amyloid formation, an unusual process in which hundreds to thousands of monomeric peptides or proteins polymerize into long, starch-like but unbranched fibrils. In addition to understanding the mechanism of amyloid formation, we have also developed therapeutic strategies, including the use of natural compounds, polymers, and nanomaterials, to prevent amyloid formation. On the other hand, we were developing methods that could be utilized to detect amyloids.
Engineering Amyloidogenic Peptides as Functional Antimicrobials
The global escalation of antibiotic resistance necessitates the development of alternative therapies, such as antimicrobial peptides (AMPs), which offer broad-spectrum activity and a lower risk of resistance development. Despite their potential, clinical translation remains limited by short half-lives and restricted administration routes. As chemists, we address these challenges by developing innovative molecular strategies that focus on islet amyloid polypeptide (IAPP), an amyloidogenic protein with demonstrated microbicidal properties. Specifically, we address the misfolding of IAPP; while historically associated with proteopathies, we seek to harness this process for beneficial "microbe agglutination", a key innate immune function that entraps and clears pathogens. Our innovative approach treats IAPP misfolding not as a byproduct, but as a functional conformational switch to provide a high-resolution thermodynamic and structural understanding of how peptide assembly can be directed for therapeutic benefit.
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Aug. 2008- Aug 2014 Ph. D., Chemistry, Stony Brook University, Stony Brook, New York
Sep. 2003- Jul. 2005 M.S., Chemistry, National Taiwan Normal University, Taipei, Taiwan