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Proteinaceous adhesive secretions from insects, and in particular the egg attachment glue of Opodiphthera sp. moths
Author(s) -
Li Dongmei,
Huson Mickey G.,
Graham Lloyd D.
Publication year - 2008
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/arch.20267
Subject(s) - biology , adhesive , glue , botany , zoology , composite material , materials science , layer (electronics)
Biochemical and electrophoretic screening of 29 adhesive secretions from Australian insects identified six types that appeared to consist largely of protein. Most were involved in terrestrial egg attachment. Hydrogel glues were subjected to gravimetric analyses and assessed for overall amino acid composition. When 32 proteins in glues from eight insect species were analyzed individually, many proved to be rich in Gly, Ser, and/or Pro, and some contained substantial levels of 4‐hydroxyproline. A few proteins were heavily glycosylated. Abundant protein‐based secretions were tested as adhesives, mainly by measuring dry shear strength on wood. The strongest (1–2 MPa) was an egg attachment glue produced by saturniid gum moths of the genus Opodiphthera . It was harvested from female colleterial gland reservoirs as a treacle‐like liquid that underwent irreversible gelation, and recovered from the capsules of laid eggs as a highly elastic orange‐brown hydrogel that could also display high tack. Its protein‐based nature was confirmed and explored by spectroscopy, enzymatic degradation, and 2D gel electrophoresis. Its proteins are mostly 80–95 kDa, and sequences (almost all novel) were established for 23 tryptic peptides. Scanning probe microscopy of Opodiphthera hydrogel in water returned median values of 0.83 nN for adhesion, 63 kPa for modulus, and 87% for resilience. Recombinant mimics of this material might be useful as biodegradable commodity adhesives or as specialty biomedical products. Arch. Insect Biochem. Physiol. 69:85–105, 2008. © 2008 Wiley‐Liss, Inc.

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