| 1. |
- Arndt, Tina, et al.
(författare)
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Engineered Spider Silk Proteins for Biomimetic Spinning of Fibers with Toughness Equal to Dragline Silks
- 2022
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Ingår i: Advanced Functional Materials. - : Wiley. - 1616-301X .- 1616-3028. ; 32:23
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Tidskriftsartikel (refereegranskat)abstract
- Spider silk is the toughest fiber found in nature, and bulk production of artificial spider silk that matches its mechanical properties remains elusive. Development of miniature spider silk proteins (mini-spidroins) has made large-scale fiber production economically feasible, but the fibers’ mechanical properties are inferior to native silk. The spider silk fiber's tensile strength is conferred by poly-alanine stretches that are zipped together by tight side chain packing in β-sheet crystals. Spidroins are secreted so they must be void of long stretches of hydrophobic residues, since such segments get inserted into the endoplasmic reticulum membrane. At the same time, hydrophobic residues have high β-strand propensity and can mediate tight inter-β-sheet interactions, features that are attractive for generation of strong artificial silks. Protein production in prokaryotes can circumvent biological laws that spiders, being eukaryotic organisms, must obey, and the authors thus design mini-spidroins that are predicted to more avidly form stronger β-sheets than the wildtype protein. Biomimetic spinning of the engineered mini-spidroins indeed results in fibers with increased tensile strength and two fiber types display toughness equal to native dragline silks. Bioreactor expression and purification result in a protein yield of ≈9 g L−1 which is in line with requirements for economically feasible bulk scale production.
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| 2. |
- Bombarda, F., et al.
(författare)
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Runaway electron beam control
- 2019
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Ingår i: Plasma Physics and Controlled Fusion. - : IOP Publishing. - 1361-6587 .- 0741-3335. ; 61:1
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Tidskriftsartikel (refereegranskat)
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| 3. |
- Bäcklund, Fredrik G., et al.
(författare)
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An Image-Analysis-Based Method for the Prediction of Recombinant Protein Fiber Tensile Strength
- 2022
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Ingår i: Materials. - : MDPI AG. - 1996-1944. ; 15:3
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Tidskriftsartikel (refereegranskat)abstract
- Silk fibers derived from the cocoon of silk moths and the wide range of silks produced by spiders exhibit an array of features, such as extraordinary tensile strength, elasticity, and adhesive properties. The functional features and mechanical properties can be derived from the structural composition and organization of the silk fibers. Artificial recombinant protein fibers based on engineered spider silk proteins have been successfully made previously and represent a promising way towards the large-scale production of fibers with predesigned features. However, for the production and use of protein fibers, there is a need for reliable objective quality control procedures that could be automated and that do not destroy the fibers in the process. Furthermore, there is still a lack of understanding the specifics of how the structural composition and organization relate to the ultimate function of silk-like fibers. In this study, we develop a new method for the categorization of protein fibers that enabled a highly accurate prediction of fiber tensile strength. Based on the use of a common light microscope equipped with polarizers together with image analysis for the precise determination of fiber morphology and optical properties, this represents an easy-to-use, objective non-destructive quality control process for protein fiber manufacturing and provides further insights into the link between the supramolecular organization and mechanical functionality of protein fibers.
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| 4. |
- Ehrenberg, Angelica, et al.
(författare)
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Accounting for strain variations and resistance mutations in the characterization of hepatitis C NS3 protease inhibitors
- 2014
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Ingår i: Journal of enzyme inhibition and medicinal chemistry (Print). - : Informa UK Limited. - 1475-6366 .- 1475-6374. ; 29:6, s. 868-876
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Tidskriftsartikel (refereegranskat)abstract
- Context: Natural strain variation and rapid resistance development makes development of broad spectrum hepatitis C virus (HCV) drugs very challenging and evaluation of inhibitor selectivity and resistance must account for differences in the catalytic properties of enzyme variants.Objective: To understand how to study selectivity and relationships between efficacy and genotype or resistant mutants for NS3 protease inhibitors.Materials and methods: The catalytic properties of NS3 protease from genotypes 1a, 1b and 3a, and their sensitivities to four structurally and mechanistically different NS3 protease inhibitors have been analysed under different experimental conditions.Results: The optimisation of buffer conditions for each protease variant enabled the comparison of their catalytic properties and sensitivities to the inhibitors. All inhibitors were most effective against genotype 1a protease, with VX-950 having the broadest selectivity.Discussion and conclusion: A new strategy for evaluation of inhibitors relevant for the discovery of broad spectrum HCV drugs was established.
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| 5. |
- Greco, G, et al.
(författare)
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Artificial and natural silk materials have high mechanical property variability regardless of sample size
- 2022
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Ingår i: Scientific reports. - : Springer Science and Business Media LLC. - 2045-2322. ; 12:1, s. 3507-
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Tidskriftsartikel (refereegranskat)abstract
- Silk fibres attract great interest in materials science for their biological and mechanical properties. Hitherto, the mechanical properties of the silk fibres have been explored mainly by tensile tests, which provide information on their strength, Young’s modulus, strain at break and toughness modulus. Several hypotheses have been based on these data, but the intrinsic and often overlooked variability of natural and artificial silk fibres makes it challenging to identify trends and correlations. In this work, we determined the mechanical properties of Bombyx mori cocoon and degummed silk, native spider silk, and artificial spider silk, and compared them with classical commercial carbon fibres using large sample sizes (from 10 to 100 fibres, in total 200 specimens per fibre type). The results confirm a substantial variability of the mechanical properties of silk fibres compared to commercial carbon fibres, as the relative standard deviation for strength and strain at break is 10–50%. Moreover, the variability does not decrease significantly when the number of tested fibres is increased, which was surprising considering the low variability frequently reported for silk fibres in the literature. Based on this, we prove that tensile testing of 10 fibres per type is representative of a silk fibre population. Finally, we show that the ideal shape of the stress–strain curve for spider silk, characterized by a pronounced exponential stiffening regime, occurs in only 25% of all tested spider silk fibres.
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| 6. |
- Greco, Gabriele, et al.
(författare)
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Influence of experimental methods on the mechanical properties of silk fibers: A systematic literature review and future road map
- 2023
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Ingår i: Biophysics reviews. - 2688-4089. ; 4
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Forskningsöversikt (refereegranskat)abstract
- Spider silk fibers are of scientific and industrial interest because of their extraordinary mechanical properties. These properties are normally determined by tensile tests, but the values obtained are dependent on the morphology of the fibers, the test conditions, and the methods by which stress and strain are calculated. Because of this, results from many studies are not directly comparable, which has led to widespread misconceptions in the field. Here, we critically review most of the reports from the past 50 years on spider silk mechanical performance and use artificial spider silk and native silks as models to highlight the effect that different experimental setups have on the fibers' mechanical properties. The results clearly illustrate the importance of carefully evaluating the tensile test methods when comparing the results from different studies. Finally, we suggest a protocol for how to perform tensile tests on silk and biobased fibers.
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| 7. |
- Greco, Gabriele, et al.
(författare)
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Properties of Biomimetic Artificial Spider Silk Fibers Tuned by PostSpin Bath Incubation
- 2020
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Ingår i: Molecules. - : MDPI AG. - 1431-5157 .- 1420-3049. ; 25:14
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Tidskriftsartikel (refereegranskat)abstract
- Efficient production of artificial spider silk fibers with properties that match its natural counterpart has still not been achieved. Recently, a biomimetic process for spinning recombinant spider silk proteins (spidroins) was presented, in which important molecular mechanisms involved in native spider silk spinning were recapitulated. However, drawbacks of these fibers included inferior mechanical properties and problems with low resistance to aqueous environments. In this work, we show that >= 5 h incubation of the fibers, in a collection bath of 500 mM NaAc and 200 mM NaCl, at pH 5 results in fibers that do not dissolve in water or phosphate buffered saline, which implies that the fibers can be used for applications that involve wet/humid conditions. Furthermore, incubation in the collection bath improved the strain at break and was associated with increased beta-sheet content, but did not affect the fiber morphology. In summary, we present a simple way to improve artificial spider silk fiber strain at break and resistance to aqueous solvents.
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| 8. |
- Greco, Gabriele, et al.
(författare)
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Tyrosine residues mediate supercontraction in biomimetic spider silk
- 2021
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Ingår i: Communications materials. - : Springer Science and Business Media LLC. - 2662-4443. ; 2:1
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Tidskriftsartikel (refereegranskat)abstract
- Exposing spider silk to wet conditions can cause supercontraction. Here, tyrosine amino acid residues within the amorphous regions are found to contribute to supercontraction, which can be controlled by protein engineering. Water and humidity severely affect the material properties of spider major ampullate silk, causing the fiber to become plasticized, contract, swell and undergo torsion. Several amino acid residue types have been proposed to be involved in this process, but the complex composition of the native fiber complicates detailed investigations. Here, we observe supercontraction in biomimetically produced artificial spider silk fibers composed of defined proteins. We found experimental evidence that proline is not the sole residue responsible for supercontraction and that tyrosine residues in the amorphous regions of the silk fiber play an important role. Furthermore, we show that the response of artificial silk fibers to humidity can be tuned, which is important for the development of materials for applications in wet environments, eg producing water resistant fibers with maximal strain at break and toughness modulus.
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| 9. |
- Jafari, Mohammad Javad, et al.
(författare)
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Force-Induced Structural Changes in Spider Silk Fibers Introduced by ATR-FTIR Spectroscopy
- 2023
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Ingår i: ACS applied polymer materials. - : American Chemical Society. - 2637-6105. ; 5:11, s. 9433-9444
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Tidskriftsartikel (refereegranskat)abstract
- Silk fibers have unique mechanical properties, and many studies of silk aim at understanding how these properties are related to secondary structure content, which often is determined by infrared spectroscopy. We report significant method-induced irreversible structural changes to both natural and synthetic spider silk fibers, derived from the widely used attenuated total reflection Fourier-transform infrared (ATR-FTIR) technique. By varying the force used to bring fibers into contact with the internal reflection elements of ATR-FTIR accessories, we observed correlated and largely irreversible changes in the secondary structure, with shape relaxation under pressure occurring within minutes. Fitting of spectral components shows that these changes agree with transformations from the alpha-helix to the beta-sheet secondary structure with possible contributions from other secondary structure elements. We further confirm the findings with IR microspectroscopy, where similar differences were seen between the pressed and unaffected regions of spider silk fibers. Our findings show that ATR-FTIR spectroscopy requires care in its use and in the interpretation of the results.
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| 10. |
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| 11. |
- Rahman, Mashuqur, 1984-, et al.
(författare)
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Enhanced detection of ATTR amyloid using a nanofibril-based assay
- 2021
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Ingår i: Amyloid. - : Taylor and Francis Ltd.. - 1350-6129 .- 1744-2818. ; 28:3, s. 158-167
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Tidskriftsartikel (refereegranskat)abstract
- More than 30 proteins and peptides have been found to form amyloid fibrils in human diseases. Fibrils formed by transthyretin (TTR) are associated with ATTR amyloidosis, affecting many vital organs, including the heart and peripheral nervous system. Congo red staining is the gold standard method for detection of amyloid deposits in tissue. However, Congo red staining and amyloid typing methods such as immunofluorescence labelling are limited to relatively large deposits. Detection of small ATTR deposits present at an early stage of the disease could enable timely treatment and prevent severe tissue damage. In this study, we developed an enhanced ATTR amyloid detection method that uses functionalised protein nanofibrils. Using this method, we achieved sensitive detection of monomeric TTR in a microplate immunoassay and immunofluorescence labelling of ex vivo tissue from two patients containing ATTR aggregates. The system's utility was confirmed on sections from a patient with AA amyloidosis and liver sections from inflamed mouse. These results suggest that the detection system constitutes important new technology for highly sensitive detection of microscopic amounts of ATTR amyloid deposited in tissue.
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| 12. |
- Schmuck, Benjamin, et al.
(författare)
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A fine-tuned composition of protein nanofibrils yields an upgraded functionality of displayed antibody binding domains
- 2017
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Ingår i: Biotechnology Journal. - : Wiley. - 1860-6768 .- 1860-7314. ; 12
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Tidskriftsartikel (refereegranskat)abstract
- Elevated performance of instruments and electronic devices is frequently attained through miniaturization of the involved components, which increases the number of functional units in a given volume. Analogously, to conquer the limitations of materials used for the purification of monoclonal antibodies and for the sensitivity of immunoassays, the support for capturing antibodies requires miniaturization. A suitable scaffold for this purpose are cross- structured protein nanofibrils, as they offer a superior surface area over volume ratio and because manipulation can be implemented genetically. To display the antibody binding Z-domain dimers (ZZ) along the surface of the fibrils and grant maximal accessibility to the functional units, the N-terminal fragments of the fibrillating translation release factor Sup35 or ureidosuccinate transporter Ure2, both from Saccharomyces cerevisae, are simultaneously fibrillated with the chimeric-proteins Sup35-ZZ and ZZ-Ure2, respectively. Optimization of the fibril composition yields a binding capacity of 1.8 mg antibody per mg fibril, which is a binding capacity that is almost 20-fold higher, compared to the commercially available affinity medium gold standard, protein A sepharose. This study lifts the craft of nanofibril functionalization to the next level, and offers a universal framework to improve biomaterials that rely on the display of functional proteins or enzymes.
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| 13. |
- Schmuck, Benjamin, et al.
(författare)
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Coupled chemistry kinetics demonstrate the utility of functionalized Sup35 amyloid nanofibrils in biocatalytic cascades
- 2019
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Ingår i: Journal of Biological Chemistry. - 0021-9258 .- 1083-351X. ; 294, s. 14966–14977-
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Tidskriftsartikel (refereegranskat)abstract
- Concerns over the environment are a central driver for designing cell-free enzymatic cascade reactions that synthesize non?petrol-based commodity compounds. An often-suggested strategy that would demonstrate the economic competitiveness of this technology is recycling of valuable enzymes through their immobilization. For this purpose, amyloid nanofibrils are an ideal scaffold to realize chemistry-free covalent enzyme immobilization on a material that offers a large surface area. However, in most instances, only single enzyme?functionalized amyloid fibrils have so far been studied. To embark on the next stage, here we displayed xylanase A, ?-xylosidase, and an aldose sugar dehydrogenase on Sup35(1?61) nanofibrils to convert beechwood xylan to xylonolactone. We characterized this enzymatic cascade by measuring the time-dependent accumulation of xylose, xylooligomers, and xylonolactone. Furthermore, we studied the effects of relative enzyme concentrations, pH, temperature, and agitation on product formation. Our investigations revealed that a modular cascade with a mixture of xylanase and ?-xylosidase, followed by product removal and separate oxidation of xylose with the aldose sugar dehydrogenase, is more productive than an enzyme mix containing all of these enzymes together. Moreover, we found that the nanofibril-coupled enzymes do not lose activity compared with their native state. These findings provide proof of concept of the feasibility of functionalized Sup35(1?61) fibrils as a molecular scaffold for biocatalytic cascades consisting of reusable enzymes that can be used in biotechnology.
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| 14. |
- Schmuck, Benjamin
(författare)
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Functionalized protein nanomaterials and their biotechnological applications
- 2018
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Doktorsavhandling (övrigt vetenskapligt/konstnärligt)abstract
- As the ribosomal synthesis of a nascent polypeptide progresses, the chain immediately undergoes folding into α-helical and β-strand secondary structure elements. While the protein matures, the polypeptide collapses into higher order constructs that ultimately form the native protein state. Since this state represents only a local minimum on the energy landscape of protein folding, the living cell has to continuously ensure an intact proteome through elaborate cellular mechanisms. However, some proteins have a high intrinsic propensity to escape these mechanisms and re-fold, which initiates protein aggregation into β-sheet rich protein nanofibrils (PNF). The accumulation of PNF in living cells can be problematic and trigger a number of diseases. Nevertheless, some organisms utilize the robustness of these aggregates to build protective shells or to form biofilms. The insight that PNF fulfil physiological functions in nature, has led to the discovery of many, biotechnological useful, material properties. PNF based materials are environmentally friendly and can be specifically designed through genetic engineering. A diameter of less than 10 nm confers an enormous surface area over volume ratio to the nanofibrils. In addition, the fibrils have mechanical properties that are similar to spider dragline silk, natures ‘high performance polymer’. To exploit these properties biotechnologically, I aimed to solve critical challenges that delay real-world applications. First, I developed a strategy that allowed me to fibrillate the proteins Sup35 and Ure2 from Saccharomyces cerevisiae in a manner that ensures a maximal functionality of the active domains displayed on the surface of the nanofibrils. Second, I designed a set of biotechnological relevant fibrils to show that our fibrillation concept is universally applicable. Therefore, I assembled fibrils with an exceptional antibody binding capacity, antibiotic degrading properties, and compiled a reaction cascade of immobilized enzymes that process xylan biomass. Third, I characterized these functionalized fibrils in detail, which goes beyond the proof-of-concept stage. Fourth, I have raised an important question that concerns the choice of the proper methodology to upscale the production of PNF, to produce economical competitive products. As a first step towards this end goal, I used the methylotrophic yeast Komagataella pastoris as a host to produce ready-to-use fibrils, which can be separated from the yeast cells using centrifugation and water. Still, additional major efforts are necessary to develop industrial-scale production methods. Another issue that awaits a solution, is the transfer of the nanofibril mechanical properties to macro-scale structures. To finally be able to close the gap between the laboratory to marketable product, a collaboration with industrial partners is required.
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| 15. |
- Schmuck, Benjamin, et al.
(författare)
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High-yield production of a super-soluble miniature spidroin for biomimetic high-performance materials
- 2021
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Ingår i: Materials Today. - : Elsevier BV. - 1369-7021 .- 1873-4103. ; 50, s. 16-23
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Tidskriftsartikel (refereegranskat)abstract
- The mechanical properties of artificial spider silks are approaching a stage where commercial applications become realistic. However, the yields of recombinant silk proteins that can be used to produce fibers with good mechanical properties are typically very low and many purification and spinning protocols still require the use of urea, hexafluoroisopropanol, and/or methanol. Thus, improved production and spinning methods with a minimal environmental impact are needed. We have previously developed a miniature spider silk protein that is characterized by high solubility in aqueous buffers and spinnability in biomimetic set-ups. In this study, we developed a production protocol that resulted in an expression level of >20 g target protein per liter in an Escherichia coli fed-batch culture, and subsequent purification under native conditions yielded 14.5 g/l. This corresponds to a nearly six-fold increase in expression levels, and a 10-fold increase in yield after purification compared to reports for recombinant spider silk proteins. Biomimetic spinning using only aqueous buffers resulted in fibers with a toughness modulus of 74 MJ/m3, which is the highest reported for biomimetically as-spun artificial silk fibers. Thus, the process described herein represents a milestone for the economic production of biomimetic silk fibers for industrial applications.
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| 16. |
- Schmuck, Benjamin, et al.
(författare)
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Impact of physio-chemical spinning conditions on the mechanical properties of biomimetic spider silk fibers
- 2022
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Ingår i: Communications Materials. - : Springer Science and Business Media LLC. - 2662-4443. ; 3
-
Tidskriftsartikel (refereegranskat)abstract
- Artificial spider silk has emerged as a biobased fiber that could replace some petroleum-based materials that are on the market today. Recent progress made it possible to produce the recombinant spider silk protein NT2RepCT at levels that would make the commercialization of fibers spun from this protein economically feasible. However, for most applications, the mechanical properties of the artificial silk fibers need to be improved. This could potentially be achieved by redesigning the spidroin, and/or by changing spinning conditions. Here, we show that several spinning parameters have a significant impact on the fibers' mechanical properties by tensile testing more than 1000 fibers produced under 92 different conditions. The most important factors that contribute to increasing the tensile strength are fast reeling speeds and/or employing post-spin stretching. Stretching in combination with optimized spinning conditions results in fibers with a strength of >250 MPa, which is the highest reported value for fibers spun using natively folded recombinant spidroins that polymerize in response to shear forces and lowered pH.The mechanical properties of spider silk are known to be dependent on spinning conditions. Here, the tensile behavior of over 1000 biomimetic spider silk fibers spun under 92 different conditions are tested, resulting in a yield strength of more than 250 MPa.
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| 17. |
- Schmuck, Benjamin, et al.
(författare)
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Production of Ready-To-Use Functionalized Sup35 Nanofibrils Secreted by Komagataella pastoris
- 2018
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Ingår i: ACS Nano. - : American Chemical Society (ACS). - 1936-0851 .- 1936-086X. ; 12, s. 9363-9371
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Tidskriftsartikel (refereegranskat)abstract
- Amyloid nanofibrils are excellent scaffolds for design-able materials that can be endowed with biotechnologically relevant functions. However, most of all excellent ideas and concepts that have been reported in the literature might never see real-world implementation in biotechnological applications. One bottleneck is the large-scale production of these materials. In this paper, we present an attempt to create a generic and scalable platform for producing ready-to-use functionalized nanofibrils directly from a eukaryotic organism. As a model material, we assembled Sup35(1-61) amyloid nanofibrils from Saccharomyces cerevisiae decorated with the Z-domain dimer, which has a high affinity toward antibody molecules. To this end, Komagataella pastoris was engineered by inserting gene copies of Sup35(1-61) and the protein chimera Sup35(1-61)-ZZ into the genome. This strain has the capability to constantly secrete amyloidogenic proteins into the extracellular medium, where the mature functionalized fibrils form, with a production yield of 35 mg/L culture. Another striking feature of this strategy is that the separation of the fibril material from the cells requires only centrifugation and resuspension in saline water. The fast production rates, minimal hands-on time, and high stability of the assembled material are some highlights that make the direct assembly of functionalized fibrils in the extracellular medium an alternative to production methods that are not suitable for large-scale production of designed amyloids.
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| 18. |
- Schmuck, Benjamin, et al.
(författare)
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The kinetics of TEM1 antibiotic degrading enzymes that are displayed on Ure2 protein nanofibrils in a flow reactor
- 2018
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Ingår i: PLoS ONE. - : Public Library of Science (PLoS). - 1932-6203. ; 13
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Tidskriftsartikel (refereegranskat)abstract
- Enzymatic functionalization of cross-beta structured protein nanofibrils has hitherto resulted in a severe reduction of the catalytic efficiency of high turnover biocatalysts. It has been speculated that steric restrictions and mass transport pose limits on the attached enzymes, but detailed kinetics analyzing this have not yet been reported. For a more comprehensive understanding, we studied protein nanofibrils endowed with TEM1, a beta-lactamase from Escherichia coll. The packing density of TEM1 along the fibrils was controlled by co-fibrillation; in other words, the N-terminal ureidosuccinate transporter Ure2(1-80) from Saccharomyces cerevisiae was simultaneously aggregated with the chimeric proteins TEM1-Ure2(1-80). The mature fibrils were trapped in a column, and the rate of ampicillin hydrolysis was recorded using a continuous substrate flow. The turnover rate was plotted as a function of substrate molecules available per enzyme per second, which demonstrated that an elevated substrate availability counteracts mass transport limitations. To analyze this data set, we derived a kinetic model, which makes it possible to easily characterize and compare enzymes packed in columns. The functional TEM1 nanofibrils possess 80% of the catalytic turnover rate compared to free TEM1 in solution. Altogether, we have created protein nanofibrils that can effectively hydrolyze beta-lactam antibiotic contaminations and provided a groundwork strategy for other highly functional enzymatic nanofibrils.
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| 19. |
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| 20. |
- Wahlberg, Elisabet, et al.
(författare)
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Identification of proteins that specifically recognize and bind protofibrillar aggregates of amyloid-β
- 2017
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Ingår i: Scientific Reports. - : Nature Publishing Group. - 2045-2322. ; 7:1
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Tidskriftsartikel (refereegranskat)abstract
- Protofibrils of the 42 amino acids long amyloid-β peptide are transient pre-fibrillar intermediates in the process of peptide aggregation into amyloid plaques and are thought to play a critical role in the pathology of Alzheimer's disease. Hence, there is a need for research reagents and potential diagnostic reagents for detection and imaging of such aggregates. Here we describe an in vitro selection of Affibody molecules that bind to protofibrils of Aβ42cc, which is a stable engineered mimic of wild type Aβ42 protofibrils. Several binders were identified that bind Aβ42cc protofibrils with low nanomolar affinities, and which also recognize wild type Aβ42 protofibrils. Dimeric head-to-tail fusion proteins with subnanomolar binding affinities, and very slow dissociation off-rates, were also constructed. A mapping of the chemical properties of the side chains onto the Affibody scaffold surface reveals three distinct adjacent surface areas of positively charged surface, nonpolar surface and a polar surface, which presumably match a corresponding surface epitope on the protofibrils. The results demonstrate that the engineered Aβ42cc is a suitable antigen for directed evolution of affinity reagents with specificity for wild type Aβ42 protofibrils.
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| 21. |
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| 22. |
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- 2018
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Ingår i: Nuclear Fusion. - : IOP Publishing. - 1741-4326 .- 0029-5515. ; 58:9
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Tidskriftsartikel (refereegranskat)
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| 23. |
-
- 2018
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Ingår i: Nuclear Fusion. - : IOP Publishing. - 1741-4326 .- 0029-5515. ; 58:1
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Forskningsöversikt (refereegranskat)
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