Physical approaches for fabrication of organized nanostructure of resilin-mimetic elastic protein rec1-resilin

Dutta, Naba K.; Choudhury, Namita Roy; Truong, My Y.; Kim, Misook; Elvin, Christopher M.; Hill, Anita J.

doi:10.1016/j.biomaterials.2009.06.019

Cited by 41 publications

(44 citation statements)

References 33 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This result has also been supported from experimental investigations using FTIR spectroscopy. [16] Nonetheless, zeta potential measurement of aqueous solutions of rec1-resilin confirms that the experimental isoelectric point (PI, zeta potential, & = 0) is observed at pH % 4.8 (Figure 2 A) compared to the theoretical value of pH 9.2 (assuming that all residues are uniformly exposed to water). This discrepancy indicates complex organization of rec1-resilin in solution, with negatively charged protein surfaces exposed to water and positively charged residues forming the core.…”

Section: Dedicated To Professor John Ralston On the Occasion Of His 6supporting

confidence: 72%

A Genetically Engineered Protein Responsive to Multiple Stimuli

et al. 2011

Self Cite

View full text Add to dashboard Cite

Section: Dedicated To Professor John Ralston On the Occasion Of His 6supporting

confidence: 72%

A Genetically Engineered Protein Responsive to Multiple Stimuli

et al. 2011

Self Cite

View full text Add to dashboard Cite

“…Furthermore, Dutta et al studied by AFM techniques the adhesion properties of a different recombinant resilin-like polypeptide to surfaces by emphasising the possibility to tune the film morphology by the physical condition of the surface. [38] …”

Section: Role Of Proline and Glycine Residuesmentioning

confidence: 97%

“…[38] RES60n peptides show a high tendency to form fibrillar structures after 12 h of incubation at room temperature ( Figure 6). Figure 5.…”

mentioning

confidence: 96%

Molecular and Supramolecular Structural Studies on Significant Repetitive Sequences of Resilin

et al. 2009

View full text Add to dashboard Cite

Resilin is a member of the family of elastomeric proteins and is found in specialised regions of the cuticle of most insects, and provides low stiffness, high strain and efficient energy storage. It is best known for its role in insect flight and the remarkable jumping ability of fleas and spittle bugs. In common with other elastomeric proteins, the recently identified Drosophila melanogaster proresilin shows glycine-rich repetitive sequences; in particular the N- and C-terminal regions of the protein are dominated by 18 repeats of a 15-residue sequence (SDTYGAPGGGNGGRP) and eleven repeats of a 13-residue sequence (GYSGGRPGGQDLG), respectively. We synthesised and analysed the molecular and supramolecular structure of some polypeptides with sequences belonging to the glycine-rich repeated domain of D. melanogaster resilin. The conformational studies performed by CD, FTIR and NMR spectroscopies pointed to the coexistence of two main conformational features, such as folded beta-turns and (quasi)extended structures (e.g., poly-L-proline II conformation) in common with other elastomeric proteins; this suggests an elasticity mechanism for resilin common to other elastomeric proteins. Our data show that also in the case of resilin, repetitive sequences are characterised by autonomous structures almost independent of the remaining parts of the molecule as already extensively found for elastin. From a supramolecular point of view, a great tendency to aggregate in fibrous structures is observed, particularly for the resilin- inspired polypeptide (PGGGN)(10). This is encouraging for the development of resilin-based biomaterials for the production of biocompatible medical devices, as well as high performing elastic materials.

show abstract

“…Thus the physical properties of the rec1-resilin protein encoded by exon 1 of D. melanogaster recombinant resilin resembled that of natural resilin. More recent studies of rec1-resilin (exon 1) demonstrated assembly on different surfaces using atomic force microscopy (AFM) for imaging [17]. This approach is potentially useful in the design of hydrogel structures with controlled morphology from resilin proteins that could be exploited as a reservoir for drugs, nanoparticles, enzymes, catalysts and sensor applications [17].…”

Section: Introductionmentioning

confidence: 99%

Recombinant exon-encoded resilins for elastomeric biomaterials

et al. 2011

View full text Add to dashboard Cite

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-mediateed dityrosine 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 dityrosine 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.

show abstract

Physical approaches for fabrication of organized nanostructure of resilin-mimetic elastic protein rec1-resilin

Cited by 41 publications

References 33 publications

A Genetically Engineered Protein Responsive to Multiple Stimuli

A Genetically Engineered Protein Responsive to Multiple Stimuli

Molecular and Supramolecular Structural Studies on Significant Repetitive Sequences of Resilin

Recombinant exon-encoded resilins for elastomeric biomaterials

Contact Info

Product

Resources

About