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Related Experiment Video

Updated: Jan 8, 2026

Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids

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Published on: March 21, 2025

Structure-activity relationships in catalytic amyloids.

Shams Aaghaz¹, Liam R Marshall¹, Ivan V Korendovych¹

¹Department of Chemistry and Biochemistry, Baylor University, One Bear Place, Waco, TX 76706, United States of America.

Journal of Inorganic Biochemistry

|December 21, 2025

Summary

Catalytic amyloids, formed from short peptides and metal ions, show tunable esterase-like activity. Minor peptide sequence changes significantly alter catalytic efficiency and substrate selectivity, matching enzyme performance.

Keywords:

Amyloid Catalysis Enzyme design Peptides Self-assembly Substrate preference

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Last Updated: Jan 8, 2026

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Area of Science:

Biochemistry
Materials Science
Catalysis

Background:

Short peptide assemblies with metal ions offer a simple platform for catalysis.
Amyloid formation is a self-assembly process with potential catalytic applications.

Purpose of the Study:

To investigate the catalytic properties of de novo amyloid forming peptides.
To understand how catalytic activity changes with different hydrolysis substrates.
To correlate catalysis with structural characteristics of peptide assemblies.

Main Methods:

Synthesized de novo amyloid forming peptides.
Assessed catalytic activity using various hydrolysis substrates.
Analyzed structure-activity relationships.
Established kinetic benchmarks (k_uncat) for a model substrate.

Main Results:

Peptide sequence modifications drastically impacted catalytic efficiency and substrate selectivity.
Developed catalytic amyloids with specific activity comparable to de novo globular enzymes.
Established kinetic benchmarks for 4-methylumbelliferyl ester hydrolysis.

Conclusions:

Catalytic amyloids exhibit tunable esterase-like activity.
Design principles for minimal peptide scaffolds with catalytic function were explored.
This work advances the understanding of amyloid catalysis and protein design.