Spontaneous patterning obtained by evaporation of Human Elastin-like Polypeptide solutions

Bandiera, Antonella; Urbani, Ranieri; Sist, Paola

doi:10.1109/iembs.2010.5626761

Cited by 4 publications

(7 citation statements)

References 21 publications

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“…Intriguingly, we have find that the self-assembling properties of the macromolecules can be exploited to achieve regular and ordered structures that enable spatial control, which is required in some specific approaches (e.g., micropatterning, controlled deposition). Under defined conditions, patterns on the mesoscale could be obtained and it has been observed that the behavior of the two macromolecules was rather different . The kinetic of the deposition mechanism underlying the process and the complexity of the biopolymer−surface interaction remain still unknown and will be the object of future investigations.…”

Section: Discussionmentioning

confidence: 97%

“…Under defined conditions, patterns on the mesoscale could be obtained and it has been observed that the behavior of the two macromolecules was rather different. 61 The kinetic of the deposition mechanism underlyingtheprocessandthecomplexityofthebiopolymer-surface interaction remain still unknown and will be the object of future investigations.…”

Section: Discussionmentioning

confidence: 99%

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Comparison of Thermal Behavior of Two Recombinantly Expressed Human Elastin-Like Polypeptides for Cell Culture Applications

2010

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Two synthetic genes that code for artificial proteins have been constructed that were modeled on the most regularly repeated hydrophobic domain of human tropoelastin. We compare the physicochemical properties of the recombinant products that differ in their primary structure; the alanine/lysine-rich cross-linking domains, which are highly conserved in mammalian tropoelastin, were either present or absent in the recombinant products. Both biopolymers showed thermoresponsive properties, and variations were observed that were dependent on solution conditions. Cell compatibility was assayed using the biopolymers as coating agents in culture experiments with a neuroblastoma cell line; cell adhesion and proliferation effects were evaluated. The cells were found to retain their neural differentiation potential. The data presented in our work support the usefulness of these versatile biopolymers for a variety of applications related to biotechnology and biomedicine.

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Section: Discussionmentioning

confidence: 97%

Section: Discussionmentioning

confidence: 99%

Comparison of Thermal Behavior of Two Recombinantly Expressed Human Elastin-Like Polypeptides for Cell Culture Applications

2010

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“…Using recombinant DNA technology, a subclass of elastin-like polypeptides has been developed and studied in our laboratory, the human elastin-like polypeptides (HELPs), whose structure is based on a repeating hexapeptide motif (Val-Ala-Pro-Gly-Val-Gly) found in human elastin. 1 HELP ( M w = 45 kDa) is encoded by a synthetic gene consisting of eight elastin-like blocks and a unique restriction site that allows in-frame cloning of any protein sequence of interest. 2 HELP is subject to a reversible phenomenon called inverse transition temperature (ITT).…”

Section: Introductionmentioning

confidence: 99%

“…The development of biopolymers based on natural protein structures holds great potential in the field of biotechnological and biomedical applications. Using recombinant DNA technology, a subclass of elastin-like polypeptides has been developed and studied in our laboratory, the human elastin-like polypeptides (HELPs), whose structure is based on a repeating hexapeptide motif (Val-Ala-Pro-Gly-Val-Gly) found in human elastin . HELP ( M w = 45 kDa) is encoded by a synthetic gene consisting of eight elastin-like blocks and a unique restriction site that allows in-frame cloning of any protein sequence of interest .…”

Section: Introductionmentioning

confidence: 99%

Macromolecular and Solution Properties of the Recombinant Fusion Protein HUG

et al. 2022

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The recombinant fusion protein HELP-UnaG (HUG) is a bifunctional product that exhibits human elastin-like polypeptide (HELP)-specific thermal behavior, defined as a reverse phase transition, and UnaG-specific bilirubin-dependent fluorescence emission. HUG provides an interesting model to understand how its two domains influence each other’s properties. Turbidimetric, calorimetric, and light scattering measurements were used to determine different parameters for the reverse temperature transition and coacervation behavior. This shows that the UnaG domain has a measurable but limited effect on the thermal properties of HELP. Although the HELP domain decreased the affinity of UnaG for bilirubin, HUG retained the property of displacing bilirubin from bovine serum albumin and thus remains one of the strongest bilirubin-binding proteins known to date. These data demonstrate that HELP can be used to create new bifunctional fusion products that pave the way for expanded technological applications.

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“…The authors concluded that the cell response is related to features that are present in both A549 phenotypes rather than to the endothelial or epithelial origin. It should be mentioned that all cell types adhered perfectly to the substrate and did not show any signs of cytotoxicity . Further studies were conducted with HELP and HELP1 in order to assess the cell biocompatibility of these recombinant polypeptides with other cell types, such as SH‐SY5Y, a human neuroblastic subclone widely used as a neuronal cell model, or a human hepatoma cell line…”

Section: Elastinmentioning

confidence: 99%

Recombinant Technology in the Development of Materials and Systems for Soft‐Tissue Repair

Girotti

Orbanić

Ibáñez‐Fonseca

et al. 2015

Adv Healthcare Materials

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The field of biomedicine is constantly investing significant research efforts in order to gain a more in-depth understanding of the mechanisms that govern the function of body compartments and to develop creative solutions for the repair and regeneration of damaged tissues.The main overall goal is to develop relatively simple systems that are able to mimic naturally occurring constructs and can therefore be used in regenerative medicine.Recombinant technology, which is widely used to obtain new tailored synthetic genes that express polymeric protein-based structures, now offers a broad range of advantages for that purpose by permitting the tuning of biological and mechanical properties depending on the 2 intended application while simultaneously ensuring adequate biocompatibility and biodegradability of the scaffold formed by the polymers. This review is focused on recombinant protein-based materials that resemble naturally occurring proteins of interest for use in soft tissue repair. An overview of recombinant biomaterials derived from elastin, silk, collagen and resilin will be given, along with a description of their characteristics and suggested applications. Current endeavors in this field are continuously providing moreimproved materials in comparison with conventional ones. As such, a great effort is being made to put these materials through clinical trials in order to favor their future use.

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Spontaneous patterning obtained by evaporation of Human Elastin-like Polypeptide solutions

Cited by 4 publications

References 21 publications

Comparison of Thermal Behavior of Two Recombinantly Expressed Human Elastin-Like Polypeptides for Cell Culture Applications

Comparison of Thermal Behavior of Two Recombinantly Expressed Human Elastin-Like Polypeptides for Cell Culture Applications

Macromolecular and Solution Properties of the Recombinant Fusion Protein HUG

Recombinant Technology in the Development of Materials and Systems for Soft‐Tissue Repair

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