Catalytic amyloids for nucleotide hydrolysis

Area of Science:

• Biochemistry
• Materials Science
• Synthetic Biology

Background:

• Minimalistic catalysts mimicking enzyme functions are developed using self-assembling peptides.
• Catalytic amyloids, a class of such assemblies, show diverse activities with potential applications in biotechnology and prebiotic chemistry.
• Understanding the mechanistic aspects and structure-function relationships of catalytic amyloids remains a challenge.

Purpose of the Study:

• To describe a methodology for producing catalytic amyloids with specific activity towards the hydrolysis of nucleotide phosphoanhydride bonds.
• To explore the design of amyloid-prone peptide sequences based on nucleotidyltransferase active sites.
• To establish a comprehensive in vitro system for characterizing these novel catalytic amyloids.

Main Methods:

• Peptide sequence design inspired by nucleotidyltransferase active sites.
• In vitro aggregation assays to confirm amyloid formation.
• Morphological characterization of amyloid structures.
• Activity assays using nucleoside and deoxynucleoside triphosphates as substrates.

Main Results:

• A methodology was established for designing and producing catalytic amyloids.
• The developed catalytic amyloids demonstrated specific activity in hydrolyzing phosphoanhydride bonds of nucleotides.
• The study provides a framework for characterizing amyloid catalysts and their functions.

Conclusions:

• The described methodology enables the creation of novel catalytic amyloids with specific enzymatic functions.
• This approach can be extended to design catalytic amyloids for a wider range of chemical transformations.
• This work contributes to the development of minimalistic catalysts and expands the applications of catalytic amyloids.