Catalytic diversity in self-propagating peptide assemblies.

Area of Science:

• Biochemistry
• Materials Science
• Chemical Biology

Background:

• Prions are protein-only infectious agents forming diverse assembled polypeptide phases like amyloid fibers.
• While prion propagation is understood, their chemical and biological functions remain largely unexplored.
• Amyloid structures are known to self-assemble but their catalytic potential is under-investigated.

Purpose of the Study:

• To engineer peptides that form well-defined amyloid phases with catalytic capabilities.
• To investigate the structure-function relationship of amyloid catalytic sites.
• To demonstrate template-directed polymerization using engineered amyloid catalysts.

Main Methods:

• Construction of simple peptides designed to self-assemble into amyloid structures.
• Characterization of amyloid phase paracrystalline surfaces for catalytic activity.
• Systematic modification of amino acid residues to control crystalline order and catalytic repertoire.
• Demonstration of template-directed polymerization using the engineered amyloid catalysts.

Main Results:

• Engineered peptides formed stable amyloid phases with defined paracrystalline surfaces.
• These amyloid surfaces demonstrated specific enantioselective catalytic activity.
• Amino acid residue modifications predictably altered catalytic function and crystalline order.
• Amyloid templates facilitated template-directed polymerization of new polymers.

Conclusions:

• Simple peptides can be engineered into functional amyloid catalysts.
• Amyloid structures offer tunable catalytic properties for chemical synthesis.
• Engineered self-propagating amyloid templates can direct the synthesis of complex materials.