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Expression and characterization of human-elastin-repeat-based temperature-responsive protein polymers for biotechnological purposes.

Antonella Bandiera·Anna Taglienti·Fulvio Micali·Bianca Pani·Marisa Tamaro·Vittorio Crescenzi·Giorgio Manzini
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Abstract

Rapid progress has been made in the design and synthesis of oligomers and polymers that emulate the properties of natural proteins. Molecular bioengineering offers the chance to design and produce artificial polymeric proteins with tailored polymeric properties. The elastin-like polypeptides are a well-defined family of polymers with noteworthy characteristic based on the VPGVG repeated motif of bovine elastin. In the human homologue, the most regular sequence is represented by the repetition of the VAPGVG hexapeptidic motif. On the basis of this sequence, a synthetic gene has been designed, cloned and expressed in Escherichia coli to obtain artificial protein polymers. The rapid one-step in-frame cloning of any biologically active sequence can be achieved directly in the expression vector, allowing further improvement of the potential of the resulting product.

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Amino Acid MotifsAmino Acid SequenceBiopolymersBiotechnologyCell Culture TechniquesCell Line, TumorCell ProliferationChromatography, AffinityChromatography, High Pressure LiquidCoated Materials, BiocompatibleElastinEscherichia coliGenetic VectorsHumansProtein EngineeringProteinsRecombinant Fusion ProteinsSpectrometry, Mass, Electrospray IonizationTemperatureJournal Article

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Antonella Bandiera, Anna Taglienti, Fulvio Micali, Bianca Pani, Marisa Tamaro, Vittorio Crescenzi, Giorgio Manzini. 2005. Expression and characterization of human-elastin-repeat-based temperature-responsive protein polymers for biotechnological purposes.. https://doi.org/10.1042/ba20050114

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