scholarly journals Unraveling a Trap-and-Trigger Mechanism in the pH-Sensitive Self-Assembly of Spider Silk Proteins

2012 ◽  
Vol 3 (5) ◽  
pp. 658-662 ◽  
Author(s):  
Jason A. Wallace ◽  
Jana K. Shen
Keyword(s):  
Self Assembly ◽  
Spider Silk ◽  
Ph Sensitive ◽  
Silk Proteins ◽  
Trigger Mechanism

Self-assembly of spider silk proteins is controlled by a pH-sensitive relay

Nature ◽  
2010 ◽  
Vol 465 (7295) ◽  
pp. 236-238 ◽  
Author(s):  
Glareh Askarieh ◽  
My Hedhammar ◽  
Kerstin Nordling ◽  
Alejandra Saenz ◽  
Cristina Casals ◽  
...  
Keyword(s):  
Self Assembly ◽  
Spider Silk ◽  
Ph Sensitive ◽  
Silk Proteins

scholarly journals Modular Protein Architectures for pH-Dependent Interactions and Switchable Assembly of Nanocellulose

2019 ◽  
Author(s):  
Sanni Voutilainen ◽  
Arja Paananen ◽  
Martina Lille ◽  
Markus Linder
Keyword(s):  
Self Assembly ◽  
Spider Silk ◽  
Cellulose Nanofibers ◽  
Ph Sensitive ◽  
Natural Systems ◽  
Novel Proteins ◽  
Wide Range ◽  
Ph Dependent ◽  
Cellulose Binding ◽  
Different Sources

<p>Protein engineering shows a wide range of possibilities for designing properties in novel materials. Following inspiration from natural systems we have studied how combinations or duplications of protein modules can be used to engineer their interactions and achieve functional properties. Here we used cellulose binding modules (CBM) coupled to spider silk N-terminal domains that dimerize in a pH-sensitive manner. We showed how the pH-sensitive switching into dimers affected cellulose binding affinity in relation to covalent coupling between CBMs. Finally, we showed how the pH-sensitive coupling could be used to assemble cellulose nanofibers in a dynamic pH-dependent way. The work shows how novel proteins can be designed by linking functional domains from widely different sources and thereby achieve new functions in the self-assembly of nanoscale materials.</p>

scholarly journals Modular Protein Architectures for pH-Dependent Interactions and Switchable Assembly of Nanocellulose

2019 ◽  
Author(s):  
Sanni Voutilainen ◽  
Arja Paananen ◽  
Martina Lille ◽  
Markus Linder
Keyword(s):  
Self Assembly ◽  
Spider Silk ◽  
Cellulose Nanofibers ◽  
Ph Sensitive ◽  
Natural Systems ◽  
Novel Proteins ◽  
Wide Range ◽  
Ph Dependent ◽  
Cellulose Binding ◽  
Different Sources

<p>Protein engineering shows a wide range of possibilities for designing properties in novel materials. Following inspiration from natural systems we have studied how combinations or duplications of protein modules can be used to engineer their interactions and achieve functional properties. Here we used cellulose binding modules (CBM) coupled to spider silk N-terminal domains that dimerize in a pH-sensitive manner. We showed how the pH-sensitive switching into dimers affected cellulose binding affinity in relation to covalent coupling between CBMs. Finally, we showed how the pH-sensitive coupling could be used to assemble cellulose nanofibers in a dynamic pH-dependent way. The work shows how novel proteins can be designed by linking functional domains from widely different sources and thereby achieve new functions in the self-assembly of nanoscale materials.</p>

Biofabrication of 3D constructs: fabrication technologies and spider silk proteins as bioinks

2015 ◽  
Vol 87 (8) ◽  
pp. 737-749 ◽  
Author(s):  
Elise DeSimone ◽  
Kristin Schacht ◽  
Tomasz Jungst ◽  
Jürgen Groll ◽  
Thomas Scheibel
Keyword(s):  
Tissue Engineering ◽  
Self Assembly ◽  
Spider Silk ◽  
High Spatial Resolution ◽  
3D Bioprinting ◽  
High Cell ◽  
Poor Control ◽  
Silk Proteins ◽  
The Past ◽  
Simultaneous Processing

AbstractDespite significant investment in tissue engineering over the past 20 years, few tissue engineered products have made it to market. One of the reasons is the poor control over the 3D arrangement of the scaffold’s components. Biofabrication is a new field of research that exploits 3D printing technologies with high spatial resolution for the simultaneous processing of cells and biomaterials into 3D constructs suitable for tissue engineering. Cell-encapsulating biomaterials used in 3D bioprinting are referred to as bioinks. This review consists of: (1) an introduction of biofabrication, (2) an introduction of 3D bioprinting, (3) the requirements of bioinks, (4) existing bioinks, and (5) a specific example of a recombinant spider silk bioink. The recombinant spider silk bioink will be used as an example because its unmodified hydrogel format fits the basic requirements of bioinks: to be printable and at the same time cytocompatible. The bioink exhibited both cytocompatible (self-assembly, high cell viability) and printable (injectable, shear-thinning, high shape fidelity) qualities. Although improvements can be made, it is clear from this system that, with the appropriate bioink, many of the existing faults in tissue-like structures produced by 3D bioprinting can be minimized.

Influence of repeat numbers on self-assembly rates of repetitive recombinant spider silk proteins

2014 ◽  
Vol 186 (3) ◽  
pp. 431-437 ◽  
Author(s):  
Martin Humenik ◽  
Michael Magdeburg ◽  
Thomas Scheibel
Keyword(s):  
Self Assembly ◽  
Spider Silk ◽  
Silk Proteins

scholarly journals Interfacial Crystallization and Supramolecular Self-Assembly of Spider Silk Inspired Protein at the Water-Air Interface

Materials ◽  
2021 ◽  
Vol 14 (15) ◽  
pp. 4239
Author(s):  
Pezhman Mohammadi ◽  
Fabian Zemke ◽  
Wolfgang Wagermaier ◽  
Markus B. Linder
Keyword(s):  
Self Assembly ◽  
Spider Silk ◽  
Assembly Process ◽  
Protein Solution ◽  
Time Resolved ◽  
Macromolecular Assembly ◽  
X Ray Scattering ◽  
Air Interface ◽  
Fundamental Research ◽  
Β Sheet

Macromolecular assembly into complex morphologies and architectural shapes is an area of fundamental research and technological innovation. In this work, we investigate the self-assembly process of recombinantly produced protein inspired by spider silk (spidroin). To elucidate the first steps of the assembly process, we examined highly concentrated and viscous pendant droplets of this protein in air. We show how the protein self-assembles and crystallizes at the water–air interface into a relatively thick and highly elastic skin. Using time-resolved in situ synchrotron X-ray scattering measurements during the drying process, we showed that the skin evolved to contain a high β-sheet amount over time. We also found that β-sheet formation strongly depended on protein concentration and relative humidity. These had a strong influence not only on the amount, but also on the ordering of these structures during the β-sheet formation process. We also showed how the skin around pendant droplets can serve as a reservoir for attaining liquid–liquid phase separation and coacervation from the dilute protein solution. Essentially, this study shows a new assembly route which could be optimized for the synthesis of new materials from a dilute protein solution and determine the properties of the final products.

scholarly journals Designing of spider silk proteins for hiPSC-based cardiac tissue engineering

2021 ◽  
pp. 100114
Author(s):  
Tilman U. Esser ◽  
Vanessa T. Trossmann ◽  
Sarah Lentz ◽  
Felix B. Engel ◽  
Thomas Scheibel
Keyword(s):  
Tissue Engineering ◽  
Spider Silk ◽  
Cardiac Tissue ◽  
Cardiac Tissue Engineering ◽  
Silk Proteins

scholarly journals Force generation by protein–DNA co-condensation

2021 ◽  
Author(s):  
Thomas Quail ◽  
Stefan Golfier ◽  
Maria Elsner ◽  
Keisuke Ishihara ◽  
Vasanthanarayan Murugesan ◽  
...  
Keyword(s):  
Optical Tweezers ◽  
Self Assembly ◽  
Spider Silk ◽  
Regulatory Elements ◽  
Heterochromatin Formation ◽  
First Order Phase Transition ◽  
Dna Strand ◽  
First Order Phase

AbstractInteractions between liquids and surfaces generate forces1,2 that are crucial for many processes in biology, physics and engineering, including the motion of insects on the surface of water3, modulation of the material properties of spider silk4 and self-assembly of microstructures5. Recent studies have shown that cells assemble biomolecular condensates via phase separation6. In the nucleus, these condensates are thought to drive transcription7, heterochromatin formation8, nucleolus assembly9 and DNA repair10. Here we show that the interaction between liquid-like condensates and DNA generates forces that might play a role in bringing distant regulatory elements of DNA together, a key step in transcriptional regulation. We combine quantitative microscopy, in vitro reconstitution, optical tweezers and theory to show that the transcription factor FoxA1 mediates the condensation of a protein–DNA phase via a mesoscopic first-order phase transition. After nucleation, co-condensation forces drive growth of this phase by pulling non-condensed DNA. Altering the tension on the DNA strand enlarges or dissolves the condensates, revealing their mechanosensitive nature. These findings show that DNA condensation mediated by transcription factors could bring distant regions of DNA into close proximity, suggesting that this physical mechanism is a possible general regulatory principle for chromatin organization that may be relevant in vivo.

Utilizing Conformational Changes for Patterning Thin Films of Recombinant Spider Silk Proteins

2012 ◽  
Vol 13 (10) ◽  
pp. 3189-3199 ◽  
Author(s):  
Seth L. Young ◽  
Maneesh Gupta ◽  
Christoph Hanske ◽  
Andreas Fery ◽  
Thomas Scheibel ◽  
...  
Keyword(s):  
Thin Films ◽  
Conformational Changes ◽  
Spider Silk ◽  
Silk Proteins
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