Multicomponent Protein Cage Co-Crystals

Información del proyecto

ProCrystal

Identificador del acuerdo de subvención: 101002258

DOI

10.3030/101002258

Fecha de la firma de la CE 20 Enero 2021

Fecha de inicio 1 Septiembre 2021

Fecha de finalización 31 Mayo 2027

Financiado con arreglo a

• EXCELLENT SCIENCE - European Research Council (ERC)

Coste total

€ 1 997 502,00

Aportación de la UE

€ 1 997 502,00

Coordinado por

AALTO KORKEAKOULUSAATIO SR
Finland

Periodic Reporting for period 3 - ProCrystal (Multicomponent Protein Cage Co-Crystals)

Período documentado: 2024-09-01 hasta 2026-02-28

Resumen del contexto y de los objetivos generales del proyecto

The development of next-generation biomaterials is critical for addressing needs related to healthcare, environmental sustainability and economic growth. However, the simple conjugation of classic synthetic materials such as polymers with biomolecules is insufficient to support the current requirements for advanced materials. Therefore, inspired by the elegant examples from living organisms on how accurately structured macromolecular systems can be realized, hierarchical and multicomponent self-assembled biomaterials are seen as reliable and efficient candidates.

Here, the strategies and fabrication methods to produce multicomponent crystals consisting of protein cages are pursued. By screening the self-assembly conditions for different protein cages and synthetic components, hierarchically ordered 3D structures with advanced functionalities are achieved, for example in catalysis, plasmonics and sequestration of chemicals. Furthermore, the understanding of the underlying principles behind the self-assembly process and the resulting structure-function relationship will shed light on the design and engineering of more complex and functional biomaterials.

Trabajo realizado desde el comienzo del proyecto hasta el final del período abarcado por el informe y los principales resultados hasta la fecha

During the project, we have synthesized the required agents for multicomponent protein cage co-crystals, including cationic ferritin and macrocycles (pillararenes and cyclodextrins). Cationic ferritin was employed to form binary crystals with negatively charged Cowpea Chlorotic Mottle Virus (CCMV) protein cages. Moreover, by incorporating gold and iron oxide particles into separate protein cages, we have explored extending the approach to create 3D magneto-plasmonic crystals. The system can be extended to ternary crystals consisting of three different particle components. We have explored a microfluidic tool to accurately control the self-assembly conditions of nanoparticles and study the solution nucleation and growth of nanoparticle co-crystals in-situ by using time-resolved SAXS. Meanwhile, the cationic macrocycles have been successfully utilized to co-crystalize with apoferritin cages for capturing inorganic and organic pollutants through host-guest chemistry. Finally, we achieved the sol-gel synthesis of mesoporous silica materials with crystalline periodicity using the apoferritin single crystals as the template. Catalytically active crystals were achieved by co-crystallizing oppositely charged ferritin nanocages, with one component encapsulating a peroxidase-mimicking enzyme. The resulting crystals exhibit long-range order, retain enzymatic activity, and can be reused in multiple catalytic cycles.

Avances que van más allá del estado de la técnica e impacto potencial esperado (incluida la repercusión socioeconómica y las implicaciones sociales más amplias del proyecto hasta la fecha)

Superlattices utilizing diverse configurations of protein cages have been extensively documented. However, creating large 3D binary nanoparticle superlattices without DNA assistance still poses a considerable challenge. Moreover, research exploring how the 3D crystal structure contributes to the distinctive functions of these materials, is yet to be conducted. This project represents an important achievement, as we have successfully synthesized 3D magnetoplasmonic crystals utilizing two distinct protein cages (ferritin and CCMV). This accomplishment is expected to provide valuable insights into both multicomponent protein crystal formation and magnetoplasmonic materials. To make this system more comprehensive, we have also prepared other 3D ordered protein crystals. These include crystals for simultaneous organic and inorganic host-guest chemistry and protein cage-templated silica growth by sol-gel chemistry. To widen the pool of available building blocks, we have used DNA-origami templating to direct the formation and assembly of various protein cages. This enables the rational design of different cage sizes and shapes, which offers and interesting starting point for preparing higher-order structures.

Cover image