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Updated: Feb 27, 2026

Non-chromatographic Purification of Recombinant Elastin-like Polypeptides and their Fusions with Peptides and Proteins from Escherichia coli

Non-chromatographic Purification of Recombinant Elastin-like Polypeptides and their Fusions with Peptides and Proteins from Escherichia coli

Published on: June 9, 2014

Elastin-like polypeptide switches: A design strategy to detect multimeric proteins.

Jugal P Dhandhukia¹, Dab A Brill¹, Aida Kouhi¹

¹Department of Pharmacology and Pharmaceutical Sciences, School of Pharmacy, University of Southern California, Los Angeles, California.

Protein Science : a Publication of the Protein Society

|June 23, 2017

Summary

This summary is machine-generated.

Elastin-like polypeptides (ELPs) can now detect large protein targets through multimerization. This advance enables the development of advanced biosensors and drug delivery systems responding to specific biological cues.

Keywords:

biotin-streptavidin stoichiometry crosslinking elastin-like polypeptides inverse phase transition temperature multimerization

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Multimer-PAGE: A Method for Capturing and Resolving Protein Complexes in Biological Samples

Multimer-PAGE: A Method for Capturing and Resolving Protein Complexes in Biological Samples

Published on: May 5, 2017

Area of Science:

Biotechnology
Materials Science
Biochemistry

Background:

Elastin-like polypeptides (ELPs) exhibit reversible phase separation triggered by environmental factors.
Current ELP applications are limited by the specificity of biological cues in microenvironments.
Developing ELP-based biosensors and drug carriers requires sensing larger protein targets.

Purpose of the Study:

To demonstrate that ELP multimerization can be engineered to detect large protein targets.
To establish a novel strategy for creating protein-responsive ELP systems.
To investigate the phase separation behavior of ELPs complexed with multimeric proteins.

Main Methods:

Biotinylation of ELPs and complexation with tetrameric streptavidin at a 4:1 stoichiometric ratio.
Characterization of ELP-streptavidin complex formation using binding affinity (K_d).
Observation of isothermal phase separation triggered by streptavidin-induced ELP multimerization.

Main Results:

Formation of stable multimeric complexes between biotin-ELPs and streptavidin with a K_d of 5 nM.
Induction of phase separation at physiological temperatures due to increased ELP density around the streptavidin core.
Reversal of phase separation upon saturation with excess streptavidin, favoring monomeric complexes.

Conclusions:

ELP multimerization is a viable strategy for detecting multimeric protein substrates.
Engineered ELPs can be designed to respond to specific protein targets.
This approach offers a pathway for developing advanced bioresponsive materials.