Silk Self-Assembly Mechanisms and Control From Thermodynamics to Kinetics

Lü, Qiang; Zhu, Hesun; Zhang, Cencen; Zhang, Feng; Zhang, Bing; Kaplan, David L.

doi:10.1021/bm201731e

Cited by 188 publications

(256 citation statements)

References 31 publications

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“…36 It is known that silk fibroin forms micellar structures in solution that transform from internal random coil conformation to betasheet structures with time. 28,29 Therefore, this conforms to the reported behavior of silk fibroin in the initial solution state. Against this background, the conformations of the RSF observed by the SAXS technique were for RSF prepared under the conditions outlined in the Experimental Section.…”

Section: Langmuirsupporting

confidence: 89%

Tunable Thermoresponsiveness of Resilin via Coassembly with Rigid Biopolymers

et al. 2015

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The ability to tune the thermoresponsiveness of recombinant resilin protein, Rec1-resilin, through a facile coassembly system was investigated in this study. The effects of change in conformation and morphology with time and the responsive behavior of Rec1-resilin in solution were studied in response to the addition of a rigid model polypeptide (poly-l-proline) or a hydrophobic rigid protein (Bombyx mori silk fibroin). It was observed that by inducing more ordered conformations and increasing the hydrophobicity the lower critical solution temperature (LCST) of the system was tuned to lower values. Time and temperature were found to be critical parameters in controlling the coassembly behavior of Rec1-resilin in both the model polypeptide and more complex protein systems. Such unique properties are useful for a wide range of applications, including drug delivery and soft tissue engineering applications.

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Section: Langmuirsupporting

confidence: 89%

Tunable Thermoresponsiveness of Resilin via Coassembly with Rigid Biopolymers

et al. 2015

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“…29 Cocoons were boiled for 20 min in an aqueous solution of 0.02 M Na 2 CO 3 and then rinsed thoroughly with distilled water to extract the sericin proteins. After drying the extracted silk fibroin was dissolved in 9.3M LiBr solution at 60°C for 4 h, yielding a 20% (w/v) solution.…”

Section: Methodsmentioning

confidence: 99%

Nanoscale control of silks for nanofibrous scaffold formation with an improved porous structure

Lin

Liu

et al. 2014

J. Mater. Chem. B

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Silk-based porous scaffolds have been used extensively in tissue engineering because of their excellent biocompatibility, tunable biodegradability and robust mechanical properties. Although many silk-based scaffolds have been prepared through freeze-drying, a challenge remains to effectively control porous structures during this process. In the present study silk fibroin with different nanostructures were self-assembled in aqueous solution by repeated drying-dissolving process and then used to improve porous structure formation in lyophilization process. Viscosity, secondary structures and water interactions were also studied to exclude their influence on the formation and control of porous structures. Following nanofiber formation in aqueous solution, silk scaffolds with improved porous structure were directly formed after lyophilization and then stabilized with water or methanol annealing treatments. Compared to silk scaffolds derived from fresh solution, the nanofibrous scaffolds showed significantly better cell compatibility in vitro. Therefore, this nanoscale control of silk offers feasible way to regulate the matrix features including porous structure and nanostructure, which are important in regulating cell and tissue outcomes in tissue engineering and regeneration, and then achieve silk-based scaffolds with improved properties.

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“…Lu and co-authors 13 propose that SF molecules form aggregates, called "micelles", with hydrophilic blocks on the surface, in contact with water, and hydrophobic blocks on the interior of the micelles. The micelles are capable of aggregating and forming fibrils due to a combination of solution concentration and electrostatic charge.…”

Section: Resultsmentioning

confidence: 99%

“…Studies indicate that regenerated SF (in aqueous solution) forms micelles, with hydrophilic blocks on the surface, in contact with water, and hydrophobic blocks inside the micelle 15 . One proposed mechanism for SF fibril formation suggests that these micelles, depending on factors such as protein concentration and charge can aggregate to form nanofibrils 13 . The stretching of the hydrophobic blocks presented inside SF micelles during the conformation transition to β-sheets is also suggested as the responsible for SF nanofibrils formation 16,17 .…”

Section: Introductionmentioning

confidence: 99%

Factors Controlling the Deposition of Silk Fibroin Nanofibrils during Layer-by-Layer Assembly

Moraes

Crouzier²,

Rubner³

et al. 2014

Biomacromolecules

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The layer-by-layer technique has been used as a powerful method to produce multilayer thin films with tunable properties. When natural polymers are employed, complicated phenomena such as self-aggregation and fibrilogenesis can occur, making it more difficult to obtain and characterize high-quality films. The weak acid and base character of such materials provides multilayer systems that may differ from those found with synthetic polymers due to strong self-organization effects. Specifically, LbL films prepared with chitosan and silk fibroin (SF) often involve the deposition of fibroin fibrils, which can influence the assembly process, surface properties, and overall film functionality. In this case, one has the intriguing possibility of realizing multilayer thin films with aligned nanofibers. In this article, we propose a strategy to control fibroin fibril formation by adjusting the assembly partner. Aligned fibroin fibrils were formed when chitosan was used as the counterpart, whereas no fibrils were observed when poly(allylamine hydrochloride) (PAH) was used. Charge density, which is higher in PAH, apparently stabilizes SF aggregates on the nanometer scale, thereby preventing their organization into fibrils. The drying step between the deposition of each layer was also crucial for film formation, as it stabilizes the SF molecules. Preliminary cell studies with optimized multilayers indicated that cell viability of NIH-3T3 fibroblasts remained between 90 and 100% after surface seeding, showing the potential application of the films in the biomedical field, as coatings and functional surfaces.

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Silk Self-Assembly Mechanisms and Control From Thermodynamics to Kinetics

Cited by 188 publications

References 31 publications

Tunable Thermoresponsiveness of Resilin via Coassembly with Rigid Biopolymers

Tunable Thermoresponsiveness of Resilin via Coassembly with Rigid Biopolymers

Nanoscale control of silks for nanofibrous scaffold formation with an improved porous structure

Factors Controlling the Deposition of Silk Fibroin Nanofibrils during Layer-by-Layer Assembly

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