| About this Abstract |
| Meeting |
2025 TMS Annual Meeting & Exhibition
|
| Symposium
|
2025 Technical Division Student Poster Contest
|
| Presentation Title |
SPU-6: Exploring the Self-Assembly of Sensory Recombinant Proteins Governed by the Phase Transition of ELP |
| Author(s) |
Adriana LaVopa, Bornita Deb, Emma McDougal, Yeongseon Jang |
| On-Site Speaker (Planned) |
Adriana LaVopa |
| Abstract Scope |
Elastin-like polypeptide (ELP) undergoes a transition from soluble to insoluble in aqueous solution above a lower critical solution temperature (LCST). This behavior enables the construction of a variety of microscale structures, such as coacervates and hollow vesicles, via thermally triggered self-assembly of ELP fusion proteins. Protein complex amphiphiles for vesicle assembly are created by genetically fusing ELP to one side of a leucine zipper motif (ZR), while hydrophilic sensory-globular proteins (FRB-mCherry, FKBP-sfGFP) are fused to the corresponding zipper motif (ZE). When exposed to a sensory analyte, the sensory proteins induce the colocalization of complementary vesicles. Vesicles were observed via epifluorescence microscopy over time and under varying analyte concentrations; statistical analyses were conducted to verify the efficacy of the sensory platform. By exploring the sensing capabilities of cell-mimetic vesicles made of ELP fusion proteins, this project contributes to biomaterials design for use in wide-reaching applications in cell therapy and drug delivery. |
| Proceedings Inclusion? |
Undecided |
| Keywords |
Biomaterials, Phase Transformations, Polymers |