Comparison between Catechol- and Thiol-Based Adhesion Using Elastin-like Polypeptides

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.