The rise in the number of daily surgical procedures and the disadvantages posed by the present surgical closure techniques (such as secondary tissue damage and microbial infection) magnifies the immediate need for metamorphosing the current bioadhesives perceiving to tether wounds efficiently. To this context, the emerging scope of biomimetics has allowed mussel inspired adhesives rendering efficient bonding characteristics on a variety of substrates. The mussel adhesion proteins and its derivatives, such as 3,4-dihydroxyphenylalanine and dopamine, are therefore widely being studied to modify the biopolymers, attempting to enhance the adhesive attributes. The polarity of the catechol groups in the protein conformation aids in the development of both noncovalent interactions (electrostatic interaction, hydrogen bonding, metal/ligand coordination bond, π-π/cation-π interactions) and covalent interactions (crosslinking), thereby promoting superior tissue adhesion. This narrative is an attempt to tether the recent developments in the mussel-inspired polymer adhesives, connecting the footprints of how these materials evolved with its current state of the art.
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