Biography

Edward (Chia-Kuei) Wu is a senior project manager and biologics/drug development project lead in the Therapeutics for Rare and Neglected Diseases (TRND) program within the Division of Preclinical Innovation, where he leads and manages early therapeutic development projects. He has more than a decade of experience in developing disease interventions, including vaccines and small-molecule therapeutics. Wu has worked on treatments for malaria and cancers, contributing to moving Investigational New Drugs into clinical studies and several U.S. patent filings.

Prior to joining NCATS in 2021, Wu was a scientific manager at the Frederick National Laboratory for Cancer Research (FNLCR), where he worked on National Cancer Institute (NCI)-funded projects developing inhibitors blocking excess interleukin-6 signaling in cancers. At FNLCR, Wu also developed a novel multiplex neutralization assay that could accelerate the testing of human papillomavirus vaccine candidates for the prevention of cervical cancers. For part of his career, Wu was the program manager for malaria transmission blocking vaccines at PATH (formerly known as Program for Appropriate Technology in Health), where he worked with the Bill & Melinda Gates Foundation and global vaccine innovators on developing next-generation malaria vaccines.

Wu received his doctorate in crystallography (structural biology) from the University of Pittsburgh, and he completed his postdoctoral training in the HIV Drug Resistance Program at NCI-Frederick.

Research Topics

Wu’s current research interest is early biologics/drug development efforts for The Helping to End Addiction Long-term^SM Initiative, or NIH HEAL Initiative^SM, and rare and neglected diseases.

Selected Publications

1. ELISA Units, IgG Subclass Ratio and Avidity Determined Functional Activity of Mouse Anti-Pfs230 Antibodies Judged by a Standard Membrane-Feeding Assay with Plasmodium Falciparum
2. An N-terminal Pfs230 Domain Produced in Baculovirus as a Biological Active Transmission-Blocking Vaccine Candidate
3. Targeting to the Endoplasmic Reticulum Improves the Folding of Recombinant Human Telomerase Reverse Transcriptase
4. The Crystal Structure of Augmenter of Liver Regeneration: A Mammalian FAD-Dependent Sulfhydryl Oxidase
5. The 2.0 Å Structure of Human Ferrochelatase, the Terminal Enzyme of Heme Biosynthesis