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Intrinsically Disordered Proteins

Intrinsically Disordered Proteins

Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...

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Related Experiment Video

Updated: Dec 26, 2025

Directed Assembly of Elastin-like Proteins into defined Supramolecular Structures and Cargo Encapsulation In Vitro

Directed Assembly of Elastin-like Proteins into defined Supramolecular Structures and Cargo Encapsulation In Vitro

Published on: April 8, 2020

Complex microparticle architectures from stimuli-responsive intrinsically disordered proteins.

Stefan Roberts¹, Vincent Miao¹, Simone Costa¹

¹Department of Biomedical Engineering, Duke University, Durham, NC, 27708, USA.

Nature Communications

|March 14, 2020

Summary

This summary is machine-generated.

Researchers developed novel protein microparticles with complex shapes using artificial intrinsically disordered proteins (IDPs). These biocompatible microparticles offer new possibilities for drug delivery and tissue engineering applications.

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Last Updated: Dec 26, 2025

Directed Assembly of Elastin-like Proteins into defined Supramolecular Structures and Cargo Encapsulation In Vitro

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Published on: April 8, 2020

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Published on: February 4, 2013

Synthesis of PolyN-isopropylacrylamide Janus Microhydrogels for Anisotropic Thermo-responsiveness and Organophilic/Hydrophilic Loading Capability

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Published on: February 27, 2016

Area of Science:

Materials Science
Bioengineering
Protein Engineering

Background:

Controllable production of microparticles with complex geometries is crucial for materials science and bioengineering.
Existing methods like flow lithography and multiple-emulsion microfluidics are sophisticated and complex.

Purpose of the Study:

To create complex microparticle geometries using artificial intrinsically disordered proteins (IDPs).
To expand the functional utility and microarchitectures of biocompatible IDPs.
To explore potential applications in drug delivery and tissue engineering.

Main Methods:

Harnessing molecular interactions of artificial intrinsically disordered proteins (IDPs).
Exploiting the metastable region of the phase diagram of thermally responsive IDPs within microdroplets.
Incorporating multi-site unnatural amino acids (UAAs) for photo-crosslinking.

Main Results:

Successfully created complex microparticle geometries including porous, core-shell, hollow-shell, and 'fruits-on-a-vine' structures.
Developed protein microparticles that can be photo-crosslinked and stably extracted to an all-aqueous environment.
Demonstrated the versatility of artificial IDPs for fabricating diverse microarchitectures.

Conclusions:

Artificial IDPs provide a versatile platform for fabricating complex microparticle architectures.
Photo-crosslinkable protein microparticles can be produced in an all-aqueous environment.
This approach offers significant potential for advanced applications in drug delivery and tissue engineering.