Elastin-like polypeptides of different molecular weights show independent transition temperatures when mixed

Teeuwen, Rosalie L. M.; Wolf, Frits A. de; Zuilhof, Han; Hest, Jan C. M. van

doi:10.1039/b909777e

Cited by 29 publications

(29 citation statements)

References 40 publications

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“…In such cases, intracellular expression is a good alternative, for example, using E. coli as an expression host. The yield of ELPs produced in E. coli is also influenced by their amino acid composition, but in agreement with the apparent compatibility of the E. coli system with low‐Tt ELPs, this influence seems smaller than in P. pastoris 21, 28, 29. ELPs with an intermediate or high Tt can be produced and secreted at relatively high yields by P. pastoris .…”

Section: Discussionsupporting

confidence: 53%

Secretion of elastin‐like polypeptides with different transition temperatures by Pichia pastoris

Schipperus

Eggink

Wolf

2011

Biotechnology Progress

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Like natural tropoelastin, polypeptides based on an elastin-like VPGXG repeat have a characteristic inverse temperature response, which leads to coacervate formation above a certain transition temperature and which could be useful for a variety of applications. The key advantage of elastin-like polypeptides (ELPs) over (tropo)elastin is a full control over this temperature response by adjustment of either the amino acid composition or the chain length, according to insights provided by extensive research. Future application of ELPs will require efficient ELP production systems, and in a previous article, we described the successful use of Pichia pastoris for secreted production of an ELP, with an overall yield of ≈ 200 mg L(-1). In this study, we investigated the influence of changed amino acid composition and chain length on the yield of secreted ELP. We have found that both parameters have a distinct impact on the overall yield, with higher yield for shorter and more hydrophilic ELPs. Because yield and transition temperature (Tt) thus appear to be positively correlated, we hypothesize that good solubility of ELP below the Tt promotes the secreted production and coacervate formation above Tt decreases it.

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Section: Discussionsupporting

confidence: 53%

Secretion of elastin‐like polypeptides with different transition temperatures by Pichia pastoris

Schipperus

Eggink

Wolf

2011

Biotechnology Progress

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“…Indeed, numerous ELPs have been expressed recombinantly in E. coli and purified. Their yields vary between 5 and 200 mg/L of culture, depending on the ELP sequence and length [10,[25][26][27][28][29][30][31]. Importantly, these ELPs were soluble during their production by the bacteria, their T t s being above 25°C at low salt concentration.…”

Section: Purification Of Elps From the Fusion Proteinmentioning

confidence: 97%

Expression and purification of short hydrophobic elastin-like polypeptides with maltose-binding protein as a solubility tag

Bataille

Dieryck

Hocquellet

et al. 2015

Protein Expression and Purification

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“…They suggested cooperative behaviour. On the other hand, Teeuwen et al [15] found that mixtures of elastin-like polypeptides with different LCST, preserved their individual transition temperatures when mixed. Other examples of the LCST behaviour of mixtures of thermoresponsive polymers are scarcely found in the literature.…”

Section: Thermal Behaviour In Aqueous Solution Of Mixtures Of P(meo 2mentioning

confidence: 99%

“…philic moieties. Undoubtedly, the most studied system is the poly(N-isopropylacrylamide), P(N-iPAAm), [9][10][11][12][13][14][15] due mainly to its sharp phase transition close to the human body temperature. However, thermoresponsive (meth)acrylic polymers containing short oligo(ethylene glycol), OEG, side chains, P(OEG x MA), were recently proposed as a very attractive alternative.…”

Section: Introductionmentioning

confidence: 99%

“…Despite that it could be a good method to tune the LCST, the solution behaviour of mixtures of different thermoresponsive polymers are scarcely found in the literature. [15,39] Furthermore, mixtures of gold nanoparticles coated with thermosensitive polymers [40] as well as nanoparticles grafted with mixtures of thermosensitive brushes [23] exhibit interesting properties that can be useful for biochemistry and sensing application. [40] The epoxy-functionalised thermosensitive block polymers present here will be used, in a future work, with this purpose.…”

Section: Introductionmentioning

confidence: 99%

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Thermoresponsive Behavior of Mixtures of Epoxy Functionalized Oligo(ethylene glycol) Methacrylate Copolymers

París

Liras

Quijada‐Garrido

2011

Macro Chemistry & Physics

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Thermoresponsive random copolymers based on 2‐(2‐methoxyethoxy)ethyl methacrylate (MEO2MA) and oligo(ethylene glycol) methyl ether methacrylate (OEG8‐9MA) are synthesized by atom transfer radical polymerization (ATRP). In a second step, they are used as macroinitiators for the ATRP of glycidyl methacrylate (GMA), introducing a short end‐block with epoxy functionalities that allows the connection of the thermoresponsive polymers to a variety of molecules, surfaces, or particles. The resulting epoxy functionalized terpolymers exhibit lower critical solution temperatures (LCST), which can be adjusted by changing the feed monomer ratio of MEO2MA and OEG8‐9MA. Binary blends show one or two cloud points depending on the blend composition. A model for the polymer collapse in one mixed particle or in two different particles as function of composition is proposed. magnified image

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Elastin-like polypeptides of different molecular weights show independent transition temperatures when mixed

Cited by 29 publications

References 40 publications

Secretion of elastin‐like polypeptides with different transition temperatures by Pichia pastoris

Secretion of elastin‐like polypeptides with different transition temperatures by Pichia pastoris

Expression and purification of short hydrophobic elastin-like polypeptides with maltose-binding protein as a solubility tag

Thermoresponsive Behavior of Mixtures of Epoxy Functionalized Oligo(ethylene glycol) Methacrylate Copolymers

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