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Fibrous Proteins

Fibrous Proteins

Fibrous proteins are either long and narrow proteins or assemble to form long and thin structures. They contain repetitive units and usually consist of either alpha helices or beta sheets and, in rare cases, a mix of both. The amino acids in the primary structure often consist of repeating amino acid sequences. The role of fibrous proteins is primarily structural. Many are located in the extracellular matrix and are present in connective tissues to impart strength and joint mobility. They are...

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Updated: Apr 28, 2026

Microfluidic Fabrication of Polymeric and Biohybrid Fibers with Predesigned Size and Shape

Microfluidic Fabrication of Polymeric and Biohybrid Fibers with Predesigned Size and Shape

Published on: January 8, 2014

Engineered coiled-coil protein microfibers.

Jasmin Hume¹, Jennifer Sun, Rudy Jacquet

¹Department of Chemical and Biomolecular Engineering, NYU Polytechnic School of Engineering , Brooklyn, New York 11201, United States.

Biomacromolecules

|June 19, 2014

Summary

This summary is machine-generated.

Researchers designed self-assembling protein microfibers that can bind small molecules. These novel biomaterials offer potential for controlled delivery applications in nanotechnology and medicine.

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Last Updated: Apr 28, 2026

Microfluidic Fabrication of Polymeric and Biohybrid Fibers with Predesigned Size and Shape

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Area of Science:

Biomaterials Science
Protein Engineering
Nanotechnology

Background:

Self-assembling protein-based biomaterials are crucial for nanotechnology and medicine.
Developing de novo proteins for controlled nano- to meso-scale assembly is a key challenge.

Purpose of the Study:

To design and characterize a novel protein engineered coiled-coil that self-assembles into microfibers.
To investigate the ability of these protein microfibers to bind hydrophobic small molecules, such as curcumin.

Main Methods:

Protein engineering of a coiled-coil structure.
Characterization of self-assembly into nanoscale and mesoscale fibers.
Assessment of small molecule binding and encapsulation capabilities.

Main Results:

Engineered protein forms nanoscale fibers from α-helical homopentameric assemblies.
Mesoscale fibers form via aggregation in the presence of curcumin.
Protein microfibers can form at remarkably low concentrations.
Fibers effectively bind curcumin, demonstrating potential for encapsulation and delivery.

Conclusions:

De novo protein engineering enables the creation of self-assembling microfibers with tunable properties.
These engineered fibers can act as depots for small molecule delivery within 3D microenvironments.
The findings open new avenues for protein-based biomaterials in drug delivery and nanotechnology.