Expression of a recombinant elastin‐like protein in <i>pichia pastoris</i>

Sallach, Rory E.; Conticello, Vincent P.; Chaikof, Elliot L.

doi:10.1002/btpr.208

Cited by 52 publications

(39 citation statements)

References 60 publications

(57 reference statements)

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“…Yeast cultures are also free from bacterial endotoxins and other cellular contaminants associated with pyrogenic pathologies that may complicate E. coli systems. 23 However, as a consequence of the more complicated eukaryotic protein production process, protein yields per cell are still reported to be lower than in similar E. coli systems, promoting research for improving protein synthesis and use of alternative yeast strains. 25 Transgenic plants are appealing hosts due to reduced cost and amenability to commercial scalability.…”

Section: Transgenic Hosts For Elp Synthesismentioning

confidence: 99%

Nano and Micro-Structures of Elastin-Like Polypeptide-Based Materials and Their Applications: Recent Developments

et al. 2013

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Elastin-like polypeptide (ELP) containing materials have spurred signi¯cant research interest for biomedical applications exploiting their biocompatible, biodegradable and nonimmunogenic nature while maintaining precise control over their chemical structure and functionality through genetic engineering. Physical, mechanical and biological properties of ELPs could be further manipulated using genetic engineering or through conjugation with a variety of chemical moieties. These chemical and physical modi¯cations also achieve interesting micro-and nanostructured ELPbased materials. Here, we review the recent developments during the past decade in the methods to engineer elastin-like materials, available genetic and chemical modi¯cation methods and applications of ELP micro and nanostructures in tissue engineering and drug delivery.

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Section: Transgenic Hosts For Elp Synthesismentioning

confidence: 99%

Nano and Micro-Structures of Elastin-Like Polypeptide-Based Materials and Their Applications: Recent Developments

et al. 2013

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“…ELP or tropoelastin production has been described in E. coli, [117] a number of plant species [118] and yeast. [119] Electrospun silk proteins have also attracted increasing interest as biopolymers in recent years due to the extreme strength of natural fibers such as spider dragline silk. Recombinant expression of spider silks is essential due to the territorial behavior of the natural hosts [120] and has been carried out in E. coli, [121] yeast, [122] silk worms, [123] and, in a scaledup production system, transgenic goats.…”

Section: Expression Systems For Recombinant Productsmentioning

confidence: 99%

Adding Functions to Biomaterial Surfaces through Protein Incorporation

et al. 2016

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The concept of biomaterials has evolved from one of inert mechanical supports with a long-term, biologically inactive role in the body into complex matrices that exhibit selective cell binding, promote proliferation and matrix production, and may ultimately become replaced by newly generated tissues in vivo. Functionalization of material surfaces with biomolecules is critical to their ability to evade immunorecognition, interact productively with surrounding tissues and extracellular matrix, and avoid bacterial colonization. Antibody molecules and their derived fragments are commonly immobilized on materials to mediate coating with specific cell types in fields such as stent endothelialization and drug delivery. The incorporation of growth factors into biomaterials has found application in promoting and accelerating bone formation in osteogenerative and related applications. Peptides and extracellular matrix proteins can impart biomolecule- and cell-specificities to materials while antimicrobial peptides have found roles in preventing biofilm formation on devices and implants. In this progress report, we detail developments in the use of diverse proteins and peptides to modify the surfaces of hard biomaterials in vivo and in vitro. Chemical approaches to immobilizing active biomolecules are presented, as well as platform technologies for isolation or generation of natural or synthetic molecules suitable for biomaterial functionalization.

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“…Others, are subjected to premature termination of translation in the presence of repetitive DNA 61 sequences or rare codons (Daly and Hearn, 2005;Sallach et al, 2009) or have a low rate of internal 62 translation initiaton (Ferreira et al, 2013;Nakamoto, 2009). A large number of studies describe the 63 conversion of proteins accumulated in inclusion bodies into soluble forms.…”

Section: Introduction 45mentioning

confidence: 99%

Strategies for the production of difficult-to-express full-length eukaryotic proteins using microbial cell factories: production of human alpha-galactosidase A

Unzueta

Vázquez

Accardi

et al. 2015

Appl Microbiol Biotechnol

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22Obtaining high levels of pure proteins remains the main bottleneck of many scientific and 23 biotechnological studies. Among all the available recombinant expression systems Escherichia coli facilitates 24 gene expression by its relative simplicity, inexpensive and fast cultivation, well-known genetics and the large 25 number of tools available for its biotechnological application. However, recombinant expression in E. coli is 26 not always a straightforward procedure and major obstacles are encountered when producing many eukaryotic 27 proteins and especially membrane proteins, linked to missing post-translational modifications, proteolysis and 28 aggregation. In this context, many conventional and unconventional eukaryotic hosts are under exploration 29 and development, but in some cases linked to complex culture media or processes. In this context, alternative 30 bacterial systems able to overcome some of the limitations posed by E. coli keeping the simplicity of 31 prokaryotic manipulation are currently emerging as convenient hosts for protein production. We have 32 comparatively produced a "difficult-to-express" human protein, the lysosomal enzyme alpha-galactosidase A 33 (hGLA) in E. coli and in the psychrophilic bacterium Pseudoalteromonas haloplanktis TAC125 cells (P. 34 halopanktis TAC125). While in E. coli the production of active hGLA was unreachable due to proteolytic 35 instability and/or protein misfolding, the expression of hGLA gene in P.halopanktis TAC125 allows obtaining 36 active enzyme. These results are discussed in the context of emerging bacterial systems for protein production 37Post-print of: Unzueta, Ugutz, et al. "Strategies for the production of difficult-to-express full-length eukaryotic proteins using microbial cell factories: production of human alpha-galactosidase

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Expression of a recombinant elastin‐like protein in pichia pastoris

Cited by 52 publications

References 60 publications

Nano and Micro-Structures of Elastin-Like Polypeptide-Based Materials and Their Applications: Recent Developments

Nano and Micro-Structures of Elastin-Like Polypeptide-Based Materials and Their Applications: Recent Developments

Adding Functions to Biomaterial Surfaces through Protein Incorporation

Strategies for the production of difficult-to-express full-length eukaryotic proteins using microbial cell factories: production of human alpha-galactosidase A

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