Animal glues are widely used in restoration as adhesives,
binders,
and consolidants for organic and inorganic materials. Their variable
performances are intrinsically linked to the adhesive properties of
collagen, which determine the chemical, physical, and mechanical properties
of the glue. We have molecularly characterized the protein components
of a range of homemade and commercial glues using mass spectrometry
techniques. A shotgun proteomic analysis provided animal origin, even
when blended, and allowed us to distinguish between hide and bone
glue on the basis of the presence of collagen type III, which is abundant
in connective skin/leather tissues and poorly synthetized in bones.
Furthermore, chemical modifications, a consequence of the preparation
protocols from the original animal tissue, were thoroughly evaluated.
Deamidation, methionine oxidation, and backbone cleavage have been
analyzed as major collagen modifications, demonstrating their variability
among different glues and showing that, on average, bone glues are
less deamidated than hide glues, but more fragmented, and mixed-collagen
glues are overall less deamidated than pure glues. We believe that
these data may be of general analytical interest in the characterization
of collagen-based materials and may help restorers in the selection
of the most appropriate materials to be used in conservation treatments.