Cross β amyloid assemblies as complex catalytic machinery.

Area of Science:

• Systems chemistry
• Biocatalysis
• Protein evolution

Background:

• The evolution of complex enzymes remains a key question in systems chemistry.
• Short peptide-based cross β amyloid sequences can form intricate structures with enzyme-like properties.
• These amyloid assemblies are proposed as potential earliest protein folds due to their catalytic proficiencies.

Purpose of the Study:

• To review recent progress in understanding the catalytic diversity of cross β amyloid assemblies.
• To highlight the influence of morphology and sequence mutations on amyloid catalysis.
• To compare amyloid catalysis with extant biological catalysts and explore future directions.

Main Methods:

• Review of laboratory and external research on cross β amyloid catalytic activities.
• Analysis of biological examples of biocatalysts.
• Comparison of amyloid assemblies with natural enzymes, including covalent catalysis, aldolase, hydrolase, and peroxidase-like activities.
• Discussion of transient catalytic amyloid phases and cytoskeleton polymerization mimicry.

Main Results:

• Cross β amyloid assemblies demonstrate a wide range of catalytic activities, including covalent catalysis, aldolase, hydrolase, and peroxidase-like functions.
• Morphology and specific mutations in peptide sequences significantly impact catalytic efficiency.
• Amyloid catalysis can be extended to complex cascade reactions and transient phases mimicking biological processes.

Conclusions:

• Short peptide-based amyloid assemblies represent promising models for early protein folds and primitive enzyme-like catalysts.
• Understanding the structure-activity relationship in these systems is crucial for designing novel catalytic networks.
• Future research in peptide-based systems chemistry can lead to robust catalytic systems with enhanced enzyme-like proficiencies and complexity.