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Review
. 2014 Apr;10(4):1612-26.
doi: 10.1016/j.actbio.2013.08.020. Epub 2013 Aug 17.

Structure-function-property-design interplay in biopolymers: spider silk

Olena Tokareva  1 , Matthew Jacobsen  2 , Markus Buehler  3 , Joyce Wong  2 , David L Kaplan  4
Affiliations
Review

Structure-function-property-design interplay in biopolymers: spider silk

Olena Tokareva et al. Acta Biomater. 2014 Apr.

Abstract

Spider silks have been a focus of research for almost two decades due to their outstanding mechanical and biophysical properties. Recent advances in genetic engineering have led to the synthesis of recombinant spider silks, thus helping to unravel a fundamental understanding of structure-function-property relationships. The relationships between molecular composition, secondary structures and mechanical properties found in different types of spider silks are described, along with a discussion of artificial spinning of these proteins and their bioapplications, including the role of silks in biomineralization and fabrication of biomaterials with controlled properties.

Keywords: Genetic engineering; Proteins; Secondary structure; Self-assembly; Spider silk.

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Figures

Figure 1
Figure 1
(a) Adult female Nephila Clavipes (golden-orb) spider provided by the Miami Metrozoo, Florida. (b) (A) Dissected major ampullate (MA) gland of the spider. The ~1 μl blob (B) protruding through a rupture of the gland wall near the spinning canal (C) was used for the rheology experiments. Modified with permission from [113].
Figure 2
Figure 2
The natural spinning process. (a) Illustration of a spider’s spinning gland divided into four parts. (b) Schematic model of the silk fiber assembly mechanism occurring along the spinning apparatus. Reproduced with permission from [3].
Figure 3
Figure 3
Silk glands, silk types and silk uses of Nephila clavipes. Reproduced with permission from [114].
Figure 4
Figure 4. Nephila clavipes
MaSp1 repeating units. Reproduced with permission and adapted from [27].
Figure 5
Figure 5
Consensus amino acid sequence of minor ampullate silk protein 1 and 2 from N. clavipes. Adapted with permission from [115] and GenBank accession no. AAC14589.
Figure 6
Figure 6
Computer models of the poly(A) and poly(GA) segments; Reprinted with permission from [28].
Figure 7
Figure 7
Computer model of the GGX repeat region; Reprinted with permission from [28]. The model is a space-filling energy-minimized antiparallel two-strand GGS region. The starting configuration was a glycine II helix for both strands.
Figure 8
Figure 8
Computer-generated model of a silk β-spiral; Reprinted with permission from [28] and 2012.igem.org. Computer-generated model of a pair of GPGQQGPGY repeats is shown. Hydrogen bonds (shown as dashed lines) occur between residues in the same β-turn and between different β-turns.
Figure 9
Figure 9
Structural motifs and their secondary structures. Reproduced with permission from [116]. The empty box marked ‘?’ indicates that the secondary structures of the ‘spacer’ motifs are unknown. MaSp1 or MaSp2: major ampullate spidroin 1 or 2; MiSp: minor ampullate spidroin; Flag: flagelliform protein.
Figure 10
Figure 10
Representative light microscope bright field image of fibers spun from recombinant spider silk in both demonstrating the effect of drawing on fiber dimensions. Scale bar is 30 μm. Reprinted with permission from [70]. Copyright 2011 American Chemical Society.
Figure 11
Figure 11
Electrospun fibroin demonstrating the nanoscale and interconnected mesh generated. Adapted with permission from [73]. Copyright 2002 American Chemical Society.
Figure 12
Figure 12
Diverse molecular assemblies of spider silk-like block copolymers in water (A, C) and 2-propanol (B). A block is represented by poly(A) repeats and B block is composed of GGX repeats.
Figure 13
Figure 13
Expression of the chimeric silkworm/spider silk/EGFP protein in (A) cocoons, (B and C) silk glands, and (D) silk fibers from spider 6-GFP silkworms. Reproduced with permission from [94].
See this image and copyright information in PMC

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