Silk‐based materials for biomedical applications

Leal‐Egaña, Aldo; Scheibel, Thomas

doi:10.1042/ba20090229

Cited by 209 publications

(183 citation statements)

References 133 publications

(177 reference statements)

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“…Silk fibroin is a biologically-derived protein polymer purified from domesticated silkworm (Bombyx mori) cocoons that has demonstrated excellent properties for biomedical applications, including biocompatibility (11)(12)(13)(14), robust mechanical strength (15), and slow, controlled degradation to nontoxic products in vivo (16). Silk can be prepared in a range of material formats, including films, hydrogels and microspheres (17,18).…”

mentioning

confidence: 99%

RETRACTED: Stabilization of vaccines and antibiotics in silk and eliminating the cold chain

Zhang

Pritchard

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

156

148

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Sensitive biological compounds, such as vaccines and antibiotics, traditionally require a time-dependent “cold chain” to maximize therapeutic activity. This flawed process results in billions of dollars worth of viable drug loss during shipping and storage, and severely limits distribution to developing nations with limited infrastructure. To address these major limitations, we demonstrate self-standing silk protein biomaterial matrices capable of stabilizing labile vaccines and antibiotics, even at temperatures up to 60 °C over more than 6 months. Initial insight into the mechanistic basis for these findings is provided. Importantly, these findings suggest a transformative approach to the cold chain to revolutionize the way many labile therapeutic drugs are stored and utilized throughout the world.

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mentioning

confidence: 99%

RETRACTED: Stabilization of vaccines and antibiotics in silk and eliminating the cold chain

Zhang

Pritchard

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

156

148

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“…Chemical cross-linking of the hydrogels (10 mg/mL protein) with ammonium peroxodisulphate and tris(2,2'-bipyridyl)dichlororuthenium(II) (a light-inducible cross-linker) yielded stable hydrogels with linear material response and much greater modulus and strength [59]. Since the spider silk hydrogels are stable over weeks and have a high elastic modulus even at low volume fractions, they are well suited for many different tissue engineering applications [60].…”

Section: Hydrogels Made From Eadf4mentioning

confidence: 99%

Recombinant Spider Silks—Biopolymers with Potential for Future Applications

2011

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Nature has evolved a range of materials that compete with man-made materials in physical properties; one of these is spider silk. Silk is a fibrous material that exhibits extremely high strength and toughness with regard to its low density. In this review we discuss the molecular structure of spider silk and how this understanding has allowed the development of recombinant silk proteins that mimic the properties of natural spider silks. Additionally, we will explore the material morphologies and the applications of these proteins. Finally, we will look at attempts to combine the silk structure with chemical polymers and how the structure of silk has inspired the engineering of novel polymers.

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“…Bombyx mori silk used in cocoons compared with dragline silk in webs). That does not mean such features could not be introduced for synthetic applications of such materials [85][86][87]. Extending the model, such a mechanism could be generic to any hierarchical fibrous material, including synthetic polymers or textiles.…”

Section: Discussionmentioning

confidence: 99%

Increasing silk fibre strength through heterogeneity of bundled fibrils

Cranford

2013

J. R. Soc. Interface.

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Can naturally arising disorder in biological materials be beneficial? Materials scientists are continuously attempting to replicate the exemplary performance of materials such as spider silk, with detailed techniques and assembly procedures. At the same time, a spider does not precisely machine silk-imaging indicates that its fibrils are heterogeneous and irregular in cross section. While past investigations either focused on the building material (e.g. the molecular scale protein sequence and behaviour) or on the ultimate structural component (e.g. silk threads and spider webs), the bundled structure of fibrils that compose spider threads has been frequently overlooked. Herein, I exploit a molecular dynamics-based coarse-grain model to construct a fully three-dimensional fibril bundle, with a length on the order of micrometres. I probe the mechanical behaviour of bundled silk fibrils with variable density of heterogenic protrusions or globules, ranging from ideally homogeneous to a saturated distribution. Subject to stretching, the model indicates that cooperativity is enhanced by contact through low-force deformation and shear 'locking' between globules, increasing shear stress transfer by up to 200 per cent. In effect, introduction of a random and disordered structure can serve to improve mechanical performance. Moreover, addition of globules allows a tuning of free volume, and thus the wettability of silk (with implications for supercontraction). These findings support the ability of silk to maintain near-molecular-level strength at the scale of silk threads, and the mechanism could be easily adopted as a strategy for synthetic fibres.

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Silk‐based materials for biomedical applications

Cited by 209 publications

References 133 publications

RETRACTED: Stabilization of vaccines and antibiotics in silk and eliminating the cold chain

RETRACTED: Stabilization of vaccines and antibiotics in silk and eliminating the cold chain

Recombinant Spider Silks—Biopolymers with Potential for Future Applications

Increasing silk fibre strength through heterogeneity of bundled fibrils

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