Characterization of a protein-based adhesive elastomer secreted by the Australian frog Notaden bennetti.
When provoked, Notaden bennetti frogs secrete an exudate which rapidly forms a tacky elastic solid ("frog glue"). This protein-based material acts as a promiscuous pressure-sensitive adhesive that functions even in wet conditions. We conducted macroscopic tests in air to assess the tensile strength of moist glue (up to 78 +/- 8 kPa) and the shear strength of dry glue (1.7 +/- 0.3 MPa). We also performed nanomechanical measurements in water to determine the adhesion (1.9-7.2 nN or greater), resilience (43-56%), and elastic modulus (170-1035 kPa) of solid glue collected in different ways. Dry glue contains little carbohydrate and consists mainly of protein. The protein complement is rich in Gly (15.8 mol %), Pro (8.8 mol %), and Glu/Gln (14.1 mol %); it also contains some 4-hydroxyproline (4.6 mol %) but no 5-hydroxylysine or 3,4-dihydroxyphenylalanine (L-Dopa). Denaturing gel electrophoresis of the glue reveals a characteristic pattern of proteins spanning 13-400 kDa. The largest protein (Nb-1R, apparent molecular mass 350-500 kDa) is also the most abundant, and this protein appears to be the key structural component. The solid glue can be dissolved in dilute acids; raising the ionic strength causes the glue components to self-assemble spontaneously into a solid which resembles the starting material. We describe scattering studies on dissolved and solid glue and provide microscopy images of glue surfaces and sections, revealing a porous interior that is consistent with the high water content (85-90 wt %) of moist glue. In addition to compositional similarities with other biological adhesives and well-known elastomeric proteins, the circular dichroism spectrum of dissolved glue is almost identical to that for soluble elastin and electron and scanning probe microscopy images invite comparison with silk fibroins. Covalent cross-linking does not seem to be necessary for the glue to set.
Graham
Lloyd D
LD
CSIRO Molecular & Health Technologies, Sydney Laboratory, P.O. Box 184, North Ryde, NSW 1670, Australia. lloyd.graham@csiro.au
Glattauer
Veronica
V
Huson
Mickey G
MG
Maxwell
Jane M
JM
Knott
Robert B
RB
White
John W
JW
Vaughan
Paul R
PR
Peng
Yong
Y
Tyler
Michael J
MJ
Werkmeister
Jerome A
JA
Ramshaw
John A
JA
D000268:Adhesiveness; D000269:Adhesives / Q000737:chemistry*; D000818:Animals; D001001:Anura / Q000378:metabolism*; D001672:Biocompatible Materials / Q000737:chemistry*; D002241:Carbohydrates / Q000737:chemistry; D002942:Circular Dichroism; D003432:Cross-Linking Reagents / Q000494:pharmacology; D004295:Dihydroxyphenylalanine / Q000737:chemistry; D020724:Elastomers / Q000737:chemistry*; D004577:Electron Probe Microanalysis; D005998:Glycine / Q000737:chemistry; D006901:Hydroxylysine / Q000737:chemistry; D006909:Hydroxyproline / Q000737:chemistry; D008027:Light; D046911:Macromolecular Substances / Q000737:chemistry*; D020527:Microscopy, Scanning Probe; D008970:Molecular Weight; D011392:Proline / Q000737:chemistry; D011506:Proteins / Q000737:chemistry; D012542:Scattering, Radiation; D013314:Stress, Mechanical; D013718:Tensile Strength; D000267:Tissue Adhesions; D014965:X-Rays
D000269:Adhesives; D001672:Biocompatible Materials; D002241:Carbohydrates; D003432:Cross-Linking Reagents; D020724:Elastomers; D046911:Macromolecular Substances; D011506:Proteins; D006901:Hydroxylysine; D004295:Dihydroxyphenylalanine; D011392:Proline; D006909:Hydroxyproline; D005998:Glycine