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Protein Folding

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...

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Updated: Jun 20, 2026

Combinatorial Synthesis of and High-throughput Protein Release from Polymer Film and Nanoparticle Libraries

Combinatorial Synthesis of and High-throughput Protein Release from Polymer Film and Nanoparticle Libraries

Published on: September 6, 2012

Restructuring Biologically Assembled Binding Protein-Biopolymer Conjugates toward Advanced Materials.

Deeptee Chandrashekhar Pande¹, Trung-Hieu Vu², Yaoying Lu¹

¹Centre for Cell Factories and Biopolymers, Griffith Institute for Biomedicine and Glycomics, Griffith University, Nathan, QLD 4111, Australia.

ACS Applied Materials & Interfaces

|December 9, 2024

Summary

Researchers restructured protein-coated biopolymer particles into new shapes like hollow spheres, fibers, and films. This process successfully retained the original protein functionality, opening new avenues for biomaterial applications.

Keywords:

biopolymer fibers films polyhydoxybutyrate spheres

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

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

Published on: April 8, 2020

Area of Science:

Biomaterials Engineering
Protein Engineering
Synthetic Biology

Background:

Bacterial cell factories can create polyhydroxybutyrate (PHB) core-shell structures with functional proteins.
These protein-polymer assemblies have potential applications in bioseparation, enzyme delivery, diagnostics, and vaccines.

Purpose of the Study:

To investigate the feasibility of dissolving and reforming protein-polymer assemblies.
To determine if protein functionality is retained after restructuring.

Main Methods:

Complete dissolution of protein-polymer assemblies in chloroform.
Reconstitution into various formats: hollow spheres, fibers, and films.
Functional assessment using green fluorescent protein (GFP) and IgG binding domains (GB1, Z domain).

Main Results:

Successful dissolution and reformation of assemblies into diverse structures.
Retention of protein functionality demonstrated by fluorescence and IgG binding assays.
The Z domain protein retained its functionality, highlighting the importance of protein refolding.

Conclusions:

Bioengineered protein-coated biopolymer particles can be dissolved and reformed into new shapes.
Protein functionality is preserved during the restructuring process.
Protein refolding properties are crucial for successful material reformation.