Yeongseon Jang » Faculty

Photo of Yeongseon Jang

Yeongseon Jang

Assistant Professor
Work Office: CHE 215 Lab: CHE 216 ​1006 Center Drive Gainesville FL 32611 Work Phone: (352) 294-1289 Website: The Jang Lab

Research Summary

MY RESEARCH GROUP SEEKS TO PROVIDE INSIGHTS AND SOLUTIONS IN THE FIELD OF SUPRAMOLECULAR BIOMATERIALS. We are aiming at engineering structural and functional properties of supramolecular biomaterials for target applications including smart capsules, micro-reactors, antibacterial and/or drug release coatings. The vision of our lab is to utilize soft matter assembly and recombinant technology for the creation of advanced biomaterials. From the deep understanding of the interactions between soft matters, including polymers, proteins, and colloids, we develop supramolecular biomaterials to present target microscopic structure, physical properties, and functionality. We also apply recombinant protein technology to rationally design functional building blocks. The supramolecular biomaterials developed in my research group include multicompartment vesicles, porous thin films, multilayer coatings, and a variety of self-assembled structures in solutions or at surfaces. 

MULTICOMPARTMENT PROTEIN VESICLES FOR PROTOCELL DEVELOPMENTWe seek to create multicompartment vesicles made from functional globular fusion proteins with controlled geometry by using microfluidics and microarrays fabricated via soft lithography. Micro-protein vesicles can carry multiple biological cargoes, which enables rational design of smart capsules for targeted drug delivery, bioreactors, and/or directional assembly to a hierarchical structure.

FUNCTIONAL PROTEIN THIN FILMS FOR CELL FATE CONTROLWe develop functional protein thin films and coatings to control cell fate at the surfaces. Thin films with controlled nanostructure (i.e., nanoscale pores or multilayers) are developed by non-solvent induced phase separation or layer-by-layer deposition with a spin-coating process. The functional protein thin films have a variety of biomedical applications, such as stem cell co-culture platforms, antibacterial surfaces, and drug release patches.

PHASE STUDY OF GLOBULAR PROTEIN-FUSED DIBLOCK COPOLYMERSWe aim to provide the fundamental understanding of the self-assembly of globular proteins fused with diblock copolymers that exhibit complex interactions. We study the phase transition/separation behavior of the globular fusion proteins in solution and at interface/surface under diverse physical and chemical stimuli, mainly using scattering and microscopic techniques. This study enables us to create new suprastructure with functional globular proteins.


Ph.D., 2013, Seoul National University
B.S., 2008, Seoul National University

Research Areas

Colloid and Surface Science
Functional Coating
Polymer Engineering
Recombinant Proteins


  • Yeongseon Jang,† Won Tae Choi,† Christopher Johnson, Andres Garcia, Preet M. Singh, Victor Breedveld, Dennis W. Hess, and Julie A. Champion, “Inhibition of Bacterial Adhesion on Nano-Textured Stainless Steel 316L by Electrochemical Etching”, ACS Biomater. Sci. Eng. 2018, 4, 90. [†Equally Contributed in This Work]
  • Yeongseon Jang, Won Tae Choi, William T. Heller, Zunlong Ke, Elizabeth R. Wright, and Julie A. Champion, “Engineering Globular Protein Vesicles through Tunable Self-Assembly of Recombinant Fusion Proteins”,Small 2017, 13, 1700399.
  • Yeongseon Jang, Woo-Sik Jang, Chen Gao, Tae Soup Shim, John C. Crocker, Daniel A. Hammer, and Daeyeon Lee “Tuning the Mechanical Properties of Recombinant Protein-Stabilized Gas Bubbles Using Triblock Copolymers”, ACS Macro Lett. 2016, 5, 371.
  • Yeongseon Jang,† Hyojin Lee,† Kookheon Char, and Jwa-Min Nam, “Transparent, Nanoporous, Transferable Membrane-Based Cell-Cell Paracrine Signaling Assay”, Adv. Mater. 2015, 27, 1893. [Inside Cover] [†Equally Contributed in This Work]
  • Yeongseon Jang, Jooyeon Seo, Bulent Akgun, Sushil Satija, and Kookheon Char, “Molecular Weight Dependence on the Disintegration of Spin-Assisted Weak Polyelectrolyte Multilayer Films”, Macromolecules 2013, 46, 4580.