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1.
PLoS One ; 6(7): e22467, 2011.
Article in English | MEDLINE | ID: mdl-21818328

ABSTRACT

Spider major ampullate silk is a high-performance biomaterial that has received much attention. However, most studies ignore plasticity in silk properties. A better understanding of silk plasticity could clarify the relative importance of chemical composition versus processing of silk dope for silk properties. It could also provide insight into how control of silk properties relates to spider ecology and silk uses. We compared silk plasticity (defined as variation in the properties of silk spun by a spider under different conditions) between three spider clades in relation to their anatomy and silk biochemistry. We found that silk plasticity exists in RTA clade and orbicularian spiders, two clades that differ in their silk biochemistry. Orbiculariae seem less dependent on external spinning conditions. They probably use a valve in their spinning duct to control friction forces and speed during spinning. Our results suggest that plasticity results from different processing of the silk dope in the spinning duct. Orbicularian spiders seem to display better control of silk properties, perhaps in relation to their more complex spinning duct valve.


Subject(s)
Ecological and Environmental Phenomena , Phylogeny , Silk/biosynthesis , Spiders/anatomy & histology , Spiders/genetics , Animals , Biomechanical Phenomena/physiology , Materials Testing , Movement , Species Specificity
2.
J Exp Biol ; 213(Pt 20): 3505-14, 2010 Oct 15.
Article in English | MEDLINE | ID: mdl-20889831

ABSTRACT

Spider silk is a promising biomaterial with impressive performance. However, some spider silks also 'supercontract' when exposed to water, shrinking by up to ∼50% in length. Supercontraction may provide a critical mechanism to tailor silk properties, both for future synthetic silk production and by the spiders themselves. Several hypotheses are proposed for the mechanism and function of supercontraction, but they remain largely untested. In particular, supercontraction may result from a rearrangement of the GPGXX motif within the silk proteins, where G represents glycine, P proline and X is one of a small subset of amino acids. Supercontraction may prevent sagging in wet orb-webs or allow spiders to tailor silk properties for different ecological functions. Because both the molecular structures of silk proteins and how dragline is used in webs differ among species, we can test these hypotheses by comparing supercontraction of silk across diverse spider taxa. In this study we measured supercontraction in 28 spider taxa, ranging from tarantulas to orb-weaving spiders. We found that silk from all species supercontracted, except that of most tarantulas. This suggests that supercontraction evolved at least with the origin of the Araneomorphae, over 200 million years ago. We found differences in the pattern of evolution for two components of supercontraction. Stress generated during supercontraction of a restrained fiber is not associated with changes in silk structure and web architecture. By contrast, the shrink of unrestrained supercontracting fibers is higher for Orbiculariae spiders, whose silk contains high ratios of GPGXX motifs. These results support the hypothesis that supercontraction is caused by a rearrangement of GPGXX motifs in silk, and that it functions to tailor silk material properties.


Subject(s)
Biological Evolution , Silk/chemistry , Silk/physiology , Spiders/chemistry , Animals , Biomechanical Phenomena , Phylogeny , Species Specificity , Spiders/classification , Spiders/genetics , Structure-Activity Relationship
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