Thermoplastic Elastomer Hydrogels via Self-Assembly of an Elastin-Mimetic Triblock Polypeptide

Protein‐based analogues of conventional thermoplastic elastomers can be designed with enhanced properties as a consequence of the precise control of primary structure. Protein 1 undergoes a reversible sol–gel transition, which results in the formation of a well‐defined elastomeric network above a lo...

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Bibliographic Details
Published in:Advanced functional materials 2002-02, Vol.12 (2), p.149-154
Main Authors: Wright, E.R., McMillan, R.A., Cooper, A., Apkarian, R.P., Conticello, V.P.
Format: Article
Language:English
Subjects:
Hydrogels
Polypeptides
Self-assembly
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Summary:Protein‐based analogues of conventional thermoplastic elastomers can be designed with enhanced properties as a consequence of the precise control of primary structure. Protein 1 undergoes a reversible sol–gel transition, which results in the formation of a well‐defined elastomeric network above a lower critical solution temperature. The morphology of the network is consistent with selective microscopic phase separation of the endblock domains. This genetic engineering approach provides a method for specification of the critical architectural parameters, such as block length and sequence, which define macromolecular properties that are important for downstream applications. Protein‐based analogues of conventional thermoplastic elastomers can be designed with enhanced properties as a consequence of the precise control of primary structure. Protein 1 (see Figure) undergoes a reversible sol–gel transition, which results in the formation of a well‐defined elastomeric network above a lower critical solution temperature.
ISSN:1616-301X
1616-3028
DOI:10.1002/1616-3028(20020201)12:2<149::AID-ADFM149>3.0.CO;2-N