Different chemistries
have been utilized for adhesive materials
to achieve adhesion in a humidified environment. l-3,4-dihydroxyphenylalanine
(DOPA) found in marine mussel adhesive proteins has generated great
interest because DOPA participates in multiple reaction mechanisms
that confer the ability to adhere in wet conditions. However, the
mussel adhesive complex also contains proteins with a relatively high
thiol content, and these proteins can contribute to adhesion through
the formation of disulfide bonds or interactions with DOPA. This work
probes the individual contributions and interactions of DOPA and thiol
chemistries to adhesion. To do so, we took advantage of the sequence
flexibility in elastin-like polypeptides (ELPs) to create model proteins
with highly similar sequences that are rich in either DOPA or thiol
residues. The sequence similarity between the two ELP adhesives allowed
us to focus on the differences between DOPA- and thiol-based adhesion.
Curing kinetics in a wet setting, capability to recover from disturbance
in the curing process, and cytocompatibility of the two adhesives
were compared. Both chemistries resulted in cytocompatible materials.
However, thiol chemistry had faster curing kinetics and higher adhesion
strengths, whereas DOPA chemistry showed better recovery from disturbances
during the curing process. By utilizing both DOPA- and thiol-based
chemistry simultaneously and adding iron ions, we achieved fast curing
kinetics, strong adhesion strengths, and good recovery from disturbances
to curing. These insights into the contribution of these chemistries
to adhesion provide important lessons for researchers designing adhesives
that work in a humid environment.