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Elastin-like polypeptides: Therapeutic applications for an emerging class of nanomedicines.


ABSTRACT: Elastin-like polypeptides (ELPs) constitute a genetically engineered class of 'protein polymers' derived from human tropoelastin. They exhibit a reversible phase separation whereby samples remain soluble below a transition temperature (Tt) but form amorphous coacervates above Tt. Their phase behavior has many possible applications in purification, sensing, activation, and nanoassembly. As humanized polypeptides, they are non-immunogenic, substrates for proteolytic biodegradation, and can be decorated with pharmacologically active peptides, proteins, and small molecules. Recombinant synthesis additionally allows precise control over ELP architecture and molecular weight, resulting in protein polymers with uniform physicochemical properties suited to the design of multifunctional biologics. As such, ELPs have been employed for various uses including as anti-cancer agents, ocular drug delivery vehicles, and protein trafficking modulators. This review aims to offer the reader a catalogue of ELPs, their various applications, and potential for commercialization across a broad spectrum of fields.

SUBMITTER: Despanie J 

PROVIDER: S-EPMC5767577 | biostudies-literature | 2016 Oct

REPOSITORIES: biostudies-literature

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Elastin-like polypeptides: Therapeutic applications for an emerging class of nanomedicines.

Despanie Jordan J   Dhandhukia Jugal P JP   Hamm-Alvarez Sarah F SF   MacKay J Andrew JA  

Journal of controlled release : official journal of the Controlled Release Society 20151111


Elastin-like polypeptides (ELPs) constitute a genetically engineered class of 'protein polymers' derived from human tropoelastin. They exhibit a reversible phase separation whereby samples remain soluble below a transition temperature (T<sub>t</sub>) but form amorphous coacervates above T<sub>t</sub>. Their phase behavior has many possible applications in purification, sensing, activation, and nanoassembly. As humanized polypeptides, they are non-immunogenic, substrates for proteolytic biodegrad  ...[more]

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