Microbial production of amino acid-modified spider dragline silk protein with intensively improved mechanical properties

Zhang, Haibo; Zhou, Fengli; Jiang, Xinglin; Cao, Mingle; Wang, Shilu; Zou, Huibin; Cao, Yujin; Xian, Ming; Liu, Huizhou

doi:10.1080/10826068.2015.1084637

Cited by 17 publications

(12 citation statements)

References 36 publications

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“…Through recombinant DNA technology, the structure and sequence of different spider silk proteins have been thoroughly studied . Meanwhile, a series of spinning methods, such as electrospinning, wet spinning, dry spinning, and melt spinning, have been developed for the fabrication of biological silks . However, the hierarchical structure of recombinant spidroins cannot be preserved well or some functional domains are absent.…”

Section: Figurementioning

confidence: 99%

Bioinspired and Mechanically Strong Fibers Based on Engineered Non‐Spider Chimeric Proteins

Sun

et al. 2020

Angew Chem Int Ed

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Silk‐protein‐based fibers have attracted considerable interest due to their low weight and extraordinary mechanical properties. Most studies on fibrous proteins focus on the recombinant spidroins, but these fibers exhibit moderate mechanical performance. Thus, the development of alternative structural proteins for the construction of robust fibers is an attractive goal. Herein, we report a class of biological fibers produced using a designed chimeric protein, which consists of the sequences of a cationic elastin‐like polypeptide and a squid ring teeth protein. Remarkably, the chimeric protein fibers exhibit a breaking strength up to about 630 MPa and a corresponding toughness as high as about 130 MJ m−3, making them superior to many recombinant spider silks and even comparable to some native counterparts. Therefore, this strategy is a novel concept for exploring bioinspired ultrastrong protein materials through the development of new types of structural chimeric proteins.

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Section: Figurementioning

confidence: 99%

Bioinspired and Mechanically Strong Fibers Based on Engineered Non‐Spider Chimeric Proteins

Sun

et al. 2020

Angew Chem Int Ed

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“…Expression of highly repetitive sequences such as the MaSp repetitive region is difficult in heterologous hosts, and therefore most constructs have been considerably smaller than the native spidroins, often including only a small part of the repetitive region and lacking one or both of the terminal domains. The water solubility levels of such constructs have still been very low (around 1% w / v [101,102]), and recombinant spidroins have therefore been dissolved in denaturing agents (reaching solubility levels of 5%–25% w / v [103,104,105]), after which spinning into tough fibers has proven difficult. In the same way that regenerated (denatured) silkworm silk cannot form fibers that are similar to native silk, it is highly unlikely that artificial fibers spun from denatured recombinant spidroins can capture the true structure and toughness of native spider silk.…”

Section: Conclusion and Future Perspectivesmentioning

confidence: 99%

Silk Spinning in Silkworms and Spiders

Andersson

Johansson

Rising

2016

IJMS

135

141

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Spiders and silkworms spin silks that outcompete the toughness of all natural and manmade fibers. Herein, we compare and contrast the spinning of silk in silkworms and spiders, with the aim of identifying features that are important for fiber formation. Although spiders and silkworms are very distantly related, some features of spinning silk seem to be universal. Both spiders and silkworms produce large silk proteins that are highly repetitive and extremely soluble at high pH, likely due to the globular terminal domains that flank an intermediate repetitive region. The silk proteins are produced and stored at a very high concentration in glands, and then transported along a narrowing tube in which they change conformation in response primarily to a pH gradient generated by carbonic anhydrase and proton pumps, as well as to ions and shear forces. The silk proteins thereby convert from random coil and alpha helical soluble conformations to beta sheet fibers. We suggest that factors that need to be optimized for successful production of artificial silk proteins capable of forming tough fibers include protein solubility, pH sensitivity, and preservation of natively folded proteins throughout the purification and initial spinning processes.

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“…When using recombinant technology, replication of the full length of recombinant spider silk proteins is oftentimes complicated, since the large length and the size of various spidroins hinder their synthesis and secretion by bacterial hosts (Teulé et al, 2009 ; Lin et al, 2013 ; Tokareva et al, 2013 ; Doblhofer et al, 2015 ; Rising and Johansson, 2015 ). The subsequent isolation and purification of spidroins is also impeded (due to the extremely low solubility compared to native spidroins) (Xu et al, 2012 ; Copeland et al, 2015 ; Zhang et al, 2015 ). Consequently, recombinant production often results in the fabrication of significantly shorter proteins with lower molecular weights that, in many cases, contain only a small portion of the repetitive region and lack one or both terminal domains (Rammensee et al, 2008 ; Heidebrecht and Scheibel, 2013 ).…”

Section: Composition–structure–property–function Relationship Of Natumentioning

confidence: 99%

Recent Advances in Development of Functional Spider Silk-Based Hybrid Materials

Kiseleva

Krivoshapkin

2020

Front. Chem.

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Silkworm silk is mainly known as a luxurious textile. Spider silk is an alternative to silkworm silk fibers and has much more outstanding properties. Silk diversity ensures variation in its application in nature and industry. This review aims to provide a critical summary of up-to-date fabrication methods of spider silk-based organic-inorganic hybrid materials. This paper focuses on the relationship between the molecular structure of spider silk and its mechanical properties. Such knowledge is essential for understanding the innate properties of spider silk as it provides insight into the sophisticated assembly processes of silk proteins into the distinct polymers as a basis for novel products. In this context, we describe the development of spider silk-based hybrids using both natural and bioengineered spider silk proteins blended with inorganic nanoparticles. The following topics are also covered: the diversity of spider silk, its composition and architecture, the differences between silkworm silk and spider silk, and the biosynthesis of natural silk. Referencing biochemical data and processes, this paper outlines the existing challenges and future outcomes.

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Microbial production of amino acid-modified spider dragline silk protein with intensively improved mechanical properties

Cited by 17 publications

References 36 publications

Bioinspired and Mechanically Strong Fibers Based on Engineered Non‐Spider Chimeric Proteins

Bioinspired and Mechanically Strong Fibers Based on Engineered Non‐Spider Chimeric Proteins

Silk Spinning in Silkworms and Spiders

Recent Advances in Development of Functional Spider Silk-Based Hybrid Materials

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