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The non-specific tissue proteins and vascular components at the glue–tissue interface represent the physical and chemical site where surgical adhesives and sealants exert their effects. This interface is composed of various extracellular matrix proteins, such as collagen and elastin, as well as plasma proteins like albumin that are present at the site of injury or surgery (Leggat et al., 2007). Surgical glues, including cyanoacrylates, fibrin sealants, and albumin-glutaraldehyde compounds, interact with these components to provide mechanical strength, seal air or fluid leaks, and promote hemostasis (Spotnitz, 2014). Because the interaction is largely non-specific and depends on the presence of functional groups like amines on the tissue surface, it is not considered a classical pharmacological target. Instead, it is a substrate for medical devices designed to facilitate wound closure and tissue repair (Passage et al., 2002). Understanding the biochemical nature of this interface is crucial for developing sealants that minimize adverse effects such as localized toxicity, excessive inflammation, or impaired healing.
Surgical glues interact with this interface through polymerization and covalent cross-linking. Cyanoacrylates undergo an exothermic reaction upon contact with moisture and ions on the tissue surface, bonding to amino groups in tissue proteins (Leggat et al., 2007). Fibrin sealants mimic the final stages of the coagulation cascade, where thrombin converts fibrinogen into a fibrin clot that adheres to the tissue (Spotnitz, 2014). Albumin-glutaraldehyde glues utilize glutaraldehyde to cross-link the bovine albumin in the glue with the lysine residues of proteins at the tissue surface (Passage et al., 2002).
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