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

Project Information

DESIRE

Grant agreement ID: 101028453

DOI

10.3030/101028453

Project closed

EC signature date 19 April 2021

Start date 1 June 2021

End date 31 May 2023

Funded under

• EXCELLENT SCIENCE - Marie Skłodowska-Curie Actions

Total cost

€ 191 149,44

EU contribution

€ 191 149,44

Coordinated by

EIDGENOESSISCHE TECHNISCHE HOCHSCHULE ZUERICH
Switzerland

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

Reporting period: 2021-06-01 to 2023-05-31

Summary of the context and overall objectives of the project

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.

Work performed from the beginning of the project to the end of the period covered by the report and main results achieved so far

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.

Progress beyond the state of the art and expected potential impact (including the socio-economic impact and the wider societal implications of the project so far)

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