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Public defense in biotechnology, Yin Yin

Public from the Aalto University School of Chemical Engineering, Department of Bioproducts and biosystems
Doctoral hat floating above a speaker's podium with a microphone

Title of the thesis: Assembly of silk-like proteins towards functional bio-inspired materials
 

Doctoral student: Yin Yin
Opponent: Professor, Kristaps Jaudzems, Latvian Institute of Organic Synthesis, Latvia
Custos: Professor Markus Linder, Aalto University School of Chemical Engineering
 

Building silk proteins for functional materials

Proteins are nature’s primary building blocks and can be assembled into advanced, sustainable, and high-performance materials that meet diverse needs. Liquid-liquid phase separation (LLPS), a prevalent phenomenon in nature, has been found involved in the organization and function of living cells and the formation of functional materials outside cells. LLPS separates mixtures into two phases: a dense phase (coacervates or condensates) and a dilute phase. This process has become important for designing new biological materials. 

In this thesis, silk-like proteins were used as building blocks to develop functional materials through LLPS, aided by the SpyCatcher-SpyTag protein pair. This research led to the development of a strong adhesive by combining silk-like proteins with mussel foot proteins. It also utilized the intrinsically disordered sequence from spider silk to selectively recruit proteins into silk-like protein-based condensates. Additionally, the study found that phosphate induces β-sheet structures in silk proteins, affecting fiber formation, and explored the assembly pathways involved in LLPS. 

Overall, this research provides strategies and insights for designing silk-based materials with specific properties, such as adhesives, selective recruitment condensates, and fibers, thereby expanding the possibilities for biomaterials inspired by nature.

Thesis available for public display 10 days prior to the defence

Yhteystiedot:
Yin Yin
[email protected]

Doctoral theses in the School of Chemical Engineering

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