Peroxidase-catalysed interfacial adhesion of aquatic caddisworm silk.
Casemaker caddisfly (Hesperophylax occidentalis) larvae use adhesive silk fibres to construct protective shelters under water. The silk comprises a distinct peripheral coating on a viscoelastic fibre core. Caddisworm silk peroxinectin (csPxt), a haem-peroxidase, was shown to be glycosylated by lectin affinity chromatography and tandem mass spectrometry. Using high-resolution H2O2 and peroxidase-dependent silver ion reduction and nanoparticle deposition, imaged by electron microscopy, csPxt activity was shown to be localized in the peripheral layer of drawn silk fibres. CsPxt catalyses dityrosine cross-linking within the adhesive peripheral layer post-draw, initiated perhaps by H2O2 generated by a silk gland-specific superoxide dismutase 3 (csSOD3) from environmental reactive oxygen species present in natural water. CsSOD3 was also shown to be a glycoprotein and is likely localized in the peripheral layer. Using a synthetic fluorescent phenolic copolymer and confocal microscopy, it was shown that csPxt catalyses oxidative cross-linking to external polyphenolic compounds capable of diffusive interpenetration into the fuzzy peripheral coating, including humic acid, a natural surface-active polyphenol. The results provide evidence of enzyme-mediated covalent cross-linking of a natural bioadhesive to polyphenol conditioned interfaces as a mechanism of permanent adhesion underwater.
Department of Bioengineering, University of Utah, Salt Lake City, UT 84112, USA.
Ching-Shuen
CS
Wang
Department of Bioengineering, University of Utah, Salt Lake City, UT 84112, USA.
Huaizhong
H
Pan
Department of Bioengineering, University of Utah, Salt Lake City, UT 84112, USA.
G Mahika
GM
Weerasekare
Department of Bioengineering, University of Utah, Salt Lake City, UT 84112, USA russell.stewart@utah.edu.
Russell J
RJ
Stewart
D000818:Animals; D001181:Arthropods / Q000737:chemistry*; D002384:Catalysis; D015815:Cell Adhesion Molecules / Q000737:chemistry*; D006861:Hydrogen Peroxide / Q000737:chemistry; D010084:Oxidation-Reduction; D009195:Peroxidase / Q000737:chemistry*; D047011:Silk / Q000737:chemistry*; D012834:Silver / Q000737:chemistry
D015815:Cell Adhesion Molecules; D047011:Silk; D012834:Silver; D006861:Hydrogen Peroxide; D009195:Peroxidase
bioadhesive; caddisworms; dityrosine cross-linking; peroxinectin; silk