Adaptation of caddisfly larval silks to aquatic habitats by phosphorylation of h-fibroin serines

Russell J. Stewart, Ching Shuen Wang

Research output: Contribution to journalArticlepeer-review

73 Citations (Scopus)

Abstract

Aquatic caddisflies diverged from a silk-spinning ancestor shared with terrestrial moths and butterflies. Caddisfly larva spin adhesive silk underwater to construct protective shelters with adventitiously gathered materials. A repeating (SX)n motif conserved in the H-fibroin of several caddisfly species is densely phosphorylated. In total, more than half of the serines in caddisfly silk may be phosphorylated. Major molecular adaptations allowing underwater spinning of an ancestral dry silk appear to have been phosphorylation of serines and the accumulation of basic residues in the silk proteins. The amphoteric nature of the silk proteins could contribute to silk fiber assembly through electrostatic association of phosphorylated blocks with arginine-rich blocks. The presence of Ca2+ in the caddisfly larval silk proteins suggest phosphorylated serines could contribute to silk fiber periodic substructure through Ca2+ crossbridging.

Original languageEnglish
Pages (from-to)969-974
Number of pages6
JournalBiomacromolecules
Volume11
Issue number4
DOIs
Publication statusPublished - Apr 12 2010

ASJC Scopus subject areas

  • Bioengineering
  • Biomaterials
  • Polymers and Plastics
  • Materials Chemistry

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