DESign of enzyme-InspiREd multivalent catalysts through functional patterning of nanosystems

Informazioni relative al progetto

DESIRE

ID dell’accordo di sovvenzione: 101028453

DOI

10.3030/101028453

Progetto chiuso

Data della firma CE 19 Aprile 2021

Data di avvio 1 Giugno 2021

Data di completamento 31 Maggio 2023

Finanziato da

• EXCELLENT SCIENCE - Marie Skłodowska-Curie Actions

Costo totale

€ 191 149,44

Contributo UE

€ 191 149,44

Coordinato da

EIDGENOESSISCHE TECHNISCHE HOCHSCHULE ZUERICH
Switzerland

Periodic Reporting for period 1 - DESIRE (DESign of enzyme-InspiREd multivalent catalysts through functional patterning of nanosystems)

Periodo di rendicontazione: 2021-06-01 al 2023-05-31

Sintesi del contesto e degli obiettivi generali del progetto

The development of artificial enzyme mimetics presents a highly promising approach to address certain drawbacks associated with natural enzymes, including their limited tolerance to varying experimental conditions, restricted substrate versatility, and limited adaptability to non-biological reactions. A recently emerged and potent strategy involves the self-assembly of peptides onto metal nanoparticles, enabling the creation of well-defined arrays of functional groups in a specific geometry and spatial arrangement. In the present project, we have successfully devised novel catalytic systems that mimic enzymes for aldol reactions and ester hydrolysis. These systems are based on silver nanoparticles coated with peptides, thereby demonstrating their efficacy as artificial catalysts.

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

A series of highly stable silver nanoparticles (AgNPs) have been synthesized in our study, and they were coated with short peptides for the purpose of investigating their catalytic potential in ester hydrolysis reactions. Multiple sets of peptidic ligands were deliberately designed to enhance local hydrophobicity, and their catalytic performances were thoroughly evaluated. These investigated systems not only feature catalytic functional groups that mimic those found in natural enzymes, but also exhibit similar characteristics, such as local hydrophobicity, spatial proximity/organization, and cooperativity, which are known to be associated with the remarkable efficiency of these natural enzyme systems.

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)

In the context of our own research efforts, we have made substantial progress in the realm of synthetic enzyme-inspired nanosystems, addressing some of the existing gaps in knowledge and understanding. Our investigations have yielded significant breakthroughs, shedding light on the design principles and mechanisms that govern the function and effectiveness of these nanosystems.
Furthermore, our research has not only contributed to the fundamental understanding of these nanosystems, but has also expanded the horizons of their practical applications. By identifying and exploring new avenues for catalytic applications, we have uncovered exciting possibilities for the use of these nanosystems as catalysts in various target reactions. These results hold immense promise and potential, as they offer novel and efficient strategies for addressing diverse chemical transformations.
Importantly, the findings from our research will serve as a valuable resource for researchers and scientists working in the field, facilitating the design and implementation of these technologies. The knowledge gained will assist in overcoming existing hurdles, enabling the development of more sophisticated and high-performing artificial enzyme mimics. Through the collaborative efforts of the scientific community, we can strive towards unlocking the full capabilities of these enzyme mimics and harnessing their transformative power in diverse domains, ranging from medicine and biotechnology to environmental sustainability and beyond.

(A) Schematic representation of peptide-coated silver nanoparticles and structure of the peptide pMB