Multicomponent Protein Cage Co-Crystals

Informazioni relative al progetto

ProCrystal

ID dell’accordo di sovvenzione: 101002258

DOI

10.3030/101002258

Data della firma CE 20 Gennaio 2021

Data di avvio 1 Settembre 2021

Data di completamento 31 Maggio 2027

Finanziato da

• EXCELLENT SCIENCE - European Research Council (ERC)

Costo totale

€ 1 997 502,00

Contributo UE

€ 1 997 502,00

Coordinato da

AALTO KORKEAKOULUSAATIO SR
Finland

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

Periodo di rendicontazione: 2024-09-01 al 2026-02-28

Sintesi del contesto e degli obiettivi generali del progetto

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.

Lavoro eseguito dall’inizio del progetto fino alla fine del periodo coperto dalla relazione e principali risultati finora ottenuti

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.

Progressi oltre lo stato dell’arte e potenziale impatto previsto (incluso l’impatto socioeconomico e le implicazioni sociali più ampie del progetto fino ad ora)

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.

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