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Amyloid Fibrils

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...

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Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly

Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly

Published on: February 6, 2020

Conformable self-assembling amyloid protein coatings with genetically programmable functionality.

Yingfeng Li¹, Ke Li¹, Xinyu Wang¹

¹Materials and Physical Biology Division, School of Physical Science and Technology, ShanghaiTech University, Shanghai 201210, China.

Science Advances

|June 4, 2020

Summary

This summary is machine-generated.

Researchers developed novel protein nanofiber coatings inspired by E. coli biofilms. These robust, versatile coatings offer substrate independence and programmable functionalities for diverse applications.

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Area of Science:

Materials Science
Biotechnology
Nanotechnology

Background:

Functional coatings are crucial for various technologies.
Existing coatings often lack robustness, substrate independence, or programmable functionalities.

Purpose of the Study:

To develop protein nanofiber coatings with substrate independence, robustness, and genetically encodable functionalities.
To demonstrate the versatility of these coatings in diverse applications.

Main Methods:

Utilized CsgA amyloid proteins from E. coli biofilms for coating fabrication.
Employed a solution-based approach for coating diverse surfaces.
Engineered protein functionalities for specific applications.

Main Results:

Achieved substrate-independent nanofiber coatings resistant to organic solvents.
Demonstrated robustness due to inherent amyloid structures.
Successfully integrated functionalities like gold enhancement, protein conjugation, and DNA binding.

Conclusions:

Developed versatile, robust, and functional protein nanofiber coatings.
Enabled proof-of-concept applications in electronics, biocatalysis, and sensors.
These coatings hold potential for advancements in multiple scientific and technological fields.