A proposed model for dragline spider silk self-assembly: Insights from the effect of the repetitive domain size on fiber properties

Biopolymers ◽  
2009 ◽  
Vol 93 (5) ◽  
pp. 458-468 ◽  
Author(s):  
Shmulik Ittah ◽  
Noaa Barak ◽  
Uri Gat
Keyword(s):  
Self Assembly ◽  
Spider Silk ◽  
Domain Size ◽  
Repetitive Domain ◽  
Fiber Properties ◽  
Proposed Model

Critical role of minor eggcase silk component in promoting spidroin chain alignment and strong fiber formation

2021 ◽  
Vol 118 (38) ◽  
pp. e2100496118
Author(s):  
Tiantian Fan ◽  
Ruiqi Qin ◽  
Yan Zhang ◽  
Jingxia Wang ◽  
Jing-Song Fan ◽  
...  
Keyword(s):  
Self Assembly ◽  
Spider Silk ◽  
Critical Role ◽  
Minor Component ◽  
Fiber Formation ◽  
Repetitive Domain ◽  
Chain Alignment ◽  
Main Components ◽  
Spider Silks

Natural spider silk with extraordinary mechanical properties is typically spun from more than one type of spidroin. Although the main components of various spider silks have been widely studied, little is known about the molecular role of the minor silk components in spidroin self-assembly and fiber formation. Here, we show that the minor component of spider eggcase silk, TuSp2, not only accelerates self-assembly but remarkably promotes molecular chain alignment of spidroins upon physical shearing. NMR structure of the repetitive domain of TuSp2 reveals that its dimeric structure with unique charged surface serves as a platform to recruit different domains of the main eggcase component TuSp1. Artificial fiber spun from the complex between TuSp1 and TuSp2 minispidroins exhibits considerably higher strength and Young’s modulus than its native counterpart. These results create a framework for rationally designing silk biomaterials based on distinct roles of silk components.

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 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.

scholarly journals Flow-Induced Self-Assembly of Spider Silk from Multi-Scale Simulations

2020 ◽  
Vol 118 (3) ◽  
pp. 479a
Author(s):  
Ana M. Herrera ◽  
Anil Kumar Dasanna ◽  
Ulrich S. Schwarz ◽  
Frauke Gräter
Keyword(s):  
Self Assembly ◽  
Spider Silk ◽  
Multi Scale

Recombinant Silk Fiber Properties Correlate to Prefibrillar Self‐Assembly

Small ◽  
2019 ◽  
Vol 15 (12) ◽  
pp. 1805294 ◽  
Author(s):  
Lingling Xu ◽  
Nathan Weatherbee‐Martin ◽  
Xiang‐Qin Liu ◽  
Jan K. Rainey
Keyword(s):  
Self Assembly ◽  
Silk Fiber ◽  
Fiber Properties

scholarly journals Biomaterials: Recombinant Silk Fiber Properties Correlate to Prefibrillar Self‐Assembly (Small 12/2019)

Small ◽  
2019 ◽  
Vol 15 (12) ◽  
pp. 1970065
Author(s):  
Lingling Xu ◽  
Nathan Weatherbee‐Martin ◽  
Xiang‐Qin Liu ◽  
Jan K. Rainey
Keyword(s):  
Self Assembly ◽  
Silk Fiber ◽  
Fiber Properties

scholarly journals Tunable structural color of bottlebrush block copolymers through direct-write 3D printing from solution

2020 ◽  
Vol 6 (24) ◽  
pp. eaaz7202 ◽  
Author(s):  
Bijal B. Patel ◽  
Dylan J. Walsh ◽  
Do Hoon Kim ◽  
Justin Kwok ◽  
Byeongdu Lee ◽  
...  
Keyword(s):  
3D Printing ◽  
Self Assembly ◽  
Three Dimensional ◽  
Size Control ◽  
Functional Materials ◽  
Domain Size ◽  
Direct Write ◽  
Processing Scheme ◽  
Solvent Vapor ◽  
Robust Processing

Additive manufacturing of functional materials is limited by control of microstructure and assembly at the nanoscale. In this work, we integrate nonequilibrium self-assembly with direct-write three-dimensional (3D) printing to prepare bottlebrush block copolymer (BBCP) photonic crystals (PCs) with tunable structure color. After varying deposition conditions during printing of a single ink solution, peak reflected wavelength for BBCP PCs span a range of 403 to 626 nm (blue to red), corresponding to an estimated change in d-spacing of >70 nm (Bragg- Snell equation). Physical characterization confirms that these vivid optical effects are underpinned by tuning of lamellar domain spacing, which we attribute to modulation of polymer conformation. Using in situ optical microscopy and solvent-vapor annealing, we identify kinetic trapping of metastable microstructures during printing as the mechanism for domain size control. More generally, we present a robust processing scheme with potential for on-the-fly property tuning of a variety of functional materials.

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>

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
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