Polymeric materials based on silk proteins

Hardy, John G.; Römer, Lin; Scheibel, Thomas

doi:10.1016/j.polymer.2008.08.006

Cited by 448 publications

(366 citation statements)

References 353 publications

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“…The possibility of employing protein aggregates as biomaterials has been considered due to the intriguing combination of biocompatibility and mechanical properties they exhibit [97,98]. A relevant example in this sense is the silk protein sericin, whose self-assembly can be directed toward objects having different fractality (such as nanofibrils, hydrogels or films) by properly changing environmental (i.e., solvent) conditions [99].…”

Section: Biomaterialsmentioning

confidence: 99%

Fractal-like structures in colloid science

Lazzari

Nicoud

Jaquet

et al. 2016

Advances in Colloid and Interface Science

162

123

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a b s t r a c tThe present work aims at reviewing our current understanding of fractal structures in the frame of colloid aggregation as well as the possibility they offer to produce novel structured materials. In particular, the existing techniques to measure and compute the fractal dimension d f are critically discussed based on the cases of organic/inorganic particles and proteins. Then the aggregation conditions affecting d f are thoroughly analyzed, pointing out the most recent literature findings and the limitations of our current understanding. Finally, the importance of the fractal dimension in applications is discussed along with possible directions for the production of new structured materials.

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Section: Biomaterialsmentioning

confidence: 99%

Fractal-like structures in colloid science

Lazzari

Nicoud

Jaquet

et al. 2016

Advances in Colloid and Interface Science

162

123

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show abstract

“…The purpose of this section is not to review such approaches, recently several excellent surveys have been published (Hardy et al, 2008;Kluge et al, 2008;Heim et al, 2009, among others and references therein), but to focus on the assessment of the existence of supercontraction in bioinspired fibers, as this property has important consequences in the design and production of artificial fibers that mimic major ampullate gland spider silks.…”

Section: Biomimetic Approachesmentioning

confidence: 99%

“…Several studies have investigated spinning of artificial dopes from engineered spider silk proteins (Lazaris et al, 2002;Hardy et al, 2008;Rammensee et al, 2008). Although very few silk genes have been completely cloned (Xia et al, 2004;Ayoub et al, 2007), due to their large size (Xu and Lewis, 1990), the existence of a small number of simple motifs of sequence extensively repeated (Gatesy et al, 2001) has led to the synthesis of artificial analogs that are believed to capture the essential features of the natural proteins, though so far no process has resulted in silk fibers that perfectly mimic the mechanical properties of natural silks.…”

Section: 2mentioning

confidence: 99%

The hidden link between supercontraction and mechanical behavior of spider silks

Calafat

Plaza

Pérez‐Rigueiro

et al. 2011

Journal of the Mechanical Behavior of Biomedical Materials

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The remarkable properties of spider silks have stimulated an increasing interest in understanding the roles of their composition and processing, as well as in the massproduction of these fibers. Previously, the variability in the mechanical properties of natural silk fibers was a major drawback in the elucidation of their behavior, but the authors have found that supercontraction of these fibers allows one to characterize and reproduce the whole range of tensile properties in a consistent way. The purpose of this review is to summarize these findings.After a review of the pertinent mechanical properties, the role of supercontraction in recovering and tailoring the tensile properties is explained, together with an alignment parameter to characterize silk fibers. The concept of the existence of a mechanical ground state is also mentioned. These behaviors can be modeled, and two such models -at the molecular and macroscopic levels -are briefly outlined. Finally, the assessment of the existence of supercontraction in bio-inspired fibers is considered, as this property may have significant consequences in the design and production of artificial fibers.

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“…Prominent examples are the byssus of mussels which contains pre-collagens as major building blocks and the silk fibers used in the cocoon of the mulberry silkworm Bombyx mori or in spider silk found in orb webs. For details see recent reviews on human collagens, 1 mussel pre-collagens, 2,3 silkworm silk, 4,5 and spider silk. [6][7][8][9] Here, we highlight some similarities concerning assembly of the proteins into fibers.…”

Section: Introductionmentioning

confidence: 99%

The role of terminal domains during storage and assembly of spider silk proteins

2011

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Fibrous proteins in nature fulfill a wide variety of functions in different structures ranging from cellular scaffolds to very resilient structures like tendons and even extra‐corporal fibers such as silks in spider webs or silkworm cocoons. Despite their different origins and sequence varieties many of these fibrous proteins share a common building principle: they consist of a large repetitive core domain flanked by relatively small non‐repetitive terminal domains. Amongst protein fibers, spider dragline silk shows prominent mechanical properties that exceed those of man‐made fibers like Kevlar. Spider silk fibers assemble in a spinning process allowing the transformation from an aqueous solution into a solid fiber within milliseconds. Here, we highlight the role of the non‐repetitive terminal domains of spider dragline silk proteins during storage in the gland and initiation of the fiber assembly process. © 2011 Wiley Periodicals, Inc. Biopolymers 97: 355–361, 2012.

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Polymeric materials based on silk proteins

Cited by 448 publications

References 353 publications

Fractal-like structures in colloid science

Fractal-like structures in colloid science

The hidden link between supercontraction and mechanical behavior of spider silks

The role of terminal domains during storage and assembly of spider silk proteins

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