Recombinant exon-encoded resilins for elastomeric biomaterials

Abstract Resilin is an elastomeric protein found in specialized regions of the cuticle of most insects, providing outstanding material properties including high resilience and fatigue lifetime for insect flight and jumping needs. Two exons (1 and 3) from the resilin gene in Drosophila melanogaster w...

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Bibliographic Details
Published in:	Biomaterials Vol. 32; no. 35; pp. 9231 - 9243
Main Authors:	Qin, Guokui, Rivkin, Amit, Lapidot, Shaul, Hu, Xiao, Preis, Itan, Arinus, Shira B, Dgany, Or, Shoseyov, Oded, Kaplan, David L
Format:	Journal Article
Language:	English
Published:	Netherlands Elsevier Ltd 01-12-2011
Subjects:	Advanced Basic Science Amino Acid Sequence Amino Acids - analysis Animals Biocompatible Materials - pharmacology Biomaterials Chromatography, High Pressure Liquid Circular Dichroism Cross-linking Cross-Linking Reagents - pharmacology Dentistry Drosophila melanogaster Drosophila melanogaster - metabolism Elasticity - drug effects Elastomer Elastomers - pharmacology Escherichia coli Exons - genetics Hydrogen Peroxide - chemistry Hydrogen Peroxide - pharmacology Insect Proteins - chemistry Insect Proteins - genetics Iron - chemistry Microscopy, Atomic Force Molecular Sequence Data Photo-Fenton Polymerization - drug effects Protein Structure, Secondary Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - isolation & purification Resilin Solubility - drug effects Spectroscopy, Fourier Transform Infrared Photo-Fenton Cross-linking Resilin Elastomer Biomaterials
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Summary:	Abstract Resilin is an elastomeric protein found in specialized regions of the cuticle of most insects, providing outstanding material properties including high resilience and fatigue lifetime for insect flight and jumping needs. Two exons (1 and 3) from the resilin gene in Drosophila melanogaster were cloned and the encoded proteins expressed as soluble products in Escherichia coli . A heat and salt precipitation method was used for efficient purification of the recombinant proteins. The proteins were solution cast from water and formed into rubber-like biomaterials via horseradish peroxidase-mediated cross-linking. Comparative studies of the two proteins expressed from the two different exons were investigated by Fourier Transform Infrared Spectroscopy (FTIR) and Circular Dichrosim (CD) for structural features. Little structural organization was found, suggesting structural order was not induced by the enzyme-mediated di-tyrosine cross-links. Atomic Force Microscopy (AFM) was used to study the elastomeric properties of the uncross-linked and cross-linked proteins. The protein from exon 1 exhibited 90% resilience in comparison to 63% for the protein from exon 3, and therefore may be the more critical domain for functional materials to mimic native resilin. Further, the cross-linking of the recombinant exon 1 via the citrate-modified photo-Fenton reaction was explored as an alternative di-tyrosine mediated polymerization method and resulted in both highly elastic and adhesive materials. The citrate-modified photo-Fenton system may be suitable for in vivo applications of resilin biomaterials.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Note: Both of the first two authors contributed equally to this work
ISSN:	0142-9612 1878-5905
DOI:	10.1016/j.biomaterials.2011.06.010