Uncovering the structure–function relationship in spider silk

Yarger, Jeffery L.; Cherry, Brian R.; Vaart, Arjan van der

doi:10.1038/natrevmats.2018.8

Cited by 270 publications

(239 citation statements)

References 156 publications

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Section: Discussionmentioning

confidence: 99%

“…The incorporation of stable isotopes, and particularly selective isotope labels, allows multinuclear and multidimensional ssNMR to determine silk structure through a combination of inter-atomic distance and torsional angle measurements and isotropic chemical shift perturbations. [40][41][42][43] Stable isotopic labeling of 2 H, 13 C, and 15 N in silk proteins for NMR analysis has been achieved by both synthesizing model peptides with isotopic amino acids, [19,44,45] as well as introducing enriched amino acids into the diet of the spinning organism. [38,46,47] In early work, cross polarization/magic angle spinning (CP/MAS) NMR and tracking of 13 C chemical shifts was proven to be useful for studying conformational changes in both silk fibroin [48] and dragline silk.…”

Section: Solid-state Nuclear Magnetic Resonancementioning

confidence: 99%

“…[119] Recent results with magnetic resonance imaging (MRI) indicate that monitoring the silk spinning process in vivo is indeed possible on live organisms, although considerable development of this method is still required before this becomes reality. [42] Continued advancements to silk protein analysis and effective utilization of a suite of analysis techniques will be essential to both early stage research as well as the development of commercially viable products as the field of advanced, silk-based materials continues to grow.…”

Section: Solid-state Samplementioning

confidence: 99%

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Experimental Methods for Characterizing the Secondary Structure and Thermal Properties of Silk Proteins

McGill

Holland

Kaplan

2018

Macromol. Rapid Commun.

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Silk proteins are biopolymers produced by spinning organisms that have been studied extensively for applications in materials engineering, regenerative medicine, and devices due to their high tensile strength and extensibility. This remarkable combination of mechanical properties arises from their unique semi-crystalline secondary structure and block copolymer features. The secondary structure of silks is highly sensitive to processing, and can be manipulated to achieve a wide array of material profiles. Studying the secondary structure of silks is therefore critical to understanding the relationship between structure and function, the strength and stability of silk-based materials, and the natural fiber synthesis process employed by spinning organisms. However, silks present unique challenges to structural characterization due to high-molecular-weight protein chains, repetitive sequences, and heterogeneity in intra- and interchain domain sizes. Here, experimental techniques used to study the secondary structure of silks, the information attainable from these techniques, and the limitations associated with them are reviewed. Ultimately, the appropriate utilization of a suite of techniques discussed here will enable detailed characterization of silk-based materials, from studying fundamental processing-structure-function relationships to developing commercially useful quality control assessments.

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Section: Discussionmentioning

confidence: 99%

Section: Solid-state Nuclear Magnetic Resonancementioning

confidence: 99%

Section: Solid-state Samplementioning

confidence: 99%

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Experimental Methods for Characterizing the Secondary Structure and Thermal Properties of Silk Proteins

McGill

Holland

Kaplan

2018

Macromol. Rapid Commun.

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“…The crystalline β‐sheet structure formed by poly(A)/poly(GA) gives rise to the high tensile strength, while amorphous domains of GGX/GPGX contribute to extensibility to silk fibers 5,12,13. The nature‐shaped combination of high strength and extensibility contributes to unraveling the outstanding mechanical toughness of the dragline silks, which are several times tougher than high performance steel and Kevlar fibers 14. In flagelliform silk proteins, the GPGGX domain is thought to give rise up to 200% of high elasticity 8.…”

Section: Species D [µM] Young's Modulus [Gpa] Strength [Mpa] Strain [mentioning

confidence: 99%

“…Structure–function relationships of most common spider silks are characterized to varying extents, and over 90% of the structural investigations on spider silk report data focus on only dragline silks 14. By contrast, despite millions of years' existent, ecological and industrial interest in spider silks, only limited silks from cylindrical gland, the outer of egg sac silks, have been characterized, as shown in Table 1 15–18.…”

Section: Species D [µM] Young's Modulus [Gpa] Strength [Mpa] Strain [mentioning

confidence: 99%

A Cuboid Spider Silk: Structure–Function Relationship and Polypeptide Signature

Kong

Wan

Dai

et al. 2020

Macromol. Rapid Commun.

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A unique cuboid spider silk from the outer egg sac of Nephila pilipes, with an unusual square cross‐section, is disclosed. The structure–function relationships within this silk are first studied through structural characterization, mechanical measurement, protein conformation, and polypeptide signature of silk proteins. This silk maintains the higher stiffness property of egg sac silks, and also shows a species difference. Environmental response of the mechanical properties within this silk are observed. Synchrotron FTIR microspectroscopy is used to monitor the silk protein conformation in a single natural silk. The β‐sheet structure aligns parallel to the fiber axis with a content of 22% ± 2.6%. The de novo resulting polypeptide from the solid silk fibers are novel, and an abundant polar amino acid insertion is observed. Short polyalanine (An, n ≤ 3), alternating serine and alanine (S/A)X, and alternating glycine and alanine (G/A)X, GGX, and SSX dominates in the resulting de novo polypeptide. This accords with the composition pattern of other egg sac silk proteins, besides the rarely observed GGX. This study broadens the library of egg sac spider silks and provides a new perspective to uncover structure–function relationships in spider silk.

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Brillouin Light Spectroscopy and Anisotropic Elasticity

Wang¹,

Fytas²

2021

Encyclopedia of Polymer Science and Technology

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Understanding the elastic properties of polymer‐based materials is essential for many applications (e.g., biofibers, coatings, interfacial fillers, organics semiconductors). Often those materials are anisotropic, posing a challenge for characterizing their direction‐dependent elasticity. As an optical technique, Brillouin light spectroscopy (BLS) allows determination of the complete elastic tensor of materials in a noncontact, nondestructive manner. The elastic properties of many polymer‐based materials have been investigated by BLS in the past five decades. In this review, we present the working principles of BLS and a few recent applications of BLS to the determination of the complete elasticity of polymer‐based, nanostructured, anisotropic materials. Considering its unique power in elasticity characterization, we expect BLS to find more applications in the future, particularly in the research fields of materials science, biomedical science, biomechanics, and nanotechnology.

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Uncovering the structure–function relationship in spider silk

Cited by 270 publications

References 156 publications

Experimental Methods for Characterizing the Secondary Structure and Thermal Properties of Silk Proteins

Experimental Methods for Characterizing the Secondary Structure and Thermal Properties of Silk Proteins

A Cuboid Spider Silk: Structure–Function Relationship and Polypeptide Signature

Brillouin Light Spectroscopy and Anisotropic Elasticity

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