From algae to barnacles, many organisms in wet environments adhere through the formation of fibrillar protein aggregates known as amyloids. These organisms secrete proteins that aggregate to form bulk adhesive materials and their successful performance could result from many beneficial properties of amyloids—insolubility, high mechanical strength, energy-dispersive peeling, and activated assembly. In the technological realm, amyloids have mainly been applied in conjunction with added adhesive chemistries. However, little is understood about how amyloids behave as adhesives. Here, we use unmodified food proteins as model systems to fabricate adhesives by curing them at the adhesive joint. We use processing conditions to control protein assembly to identify the effect of amyloids on performance. Using thermal processing, we fabricate adhesives approaching the underwater lap shear strength of commercial marine and contemporary bioinspired chemistries. Though we find differences in adhesive behavior between the examined proteins, the presence of amyloids improves underwater performance for a given protein. As many proteins can form amyloids under the proper conditions, our results encourage further research into <i>in situ</i> self-assembled protein adhesives across proteins of varying chemistry.

Bioinspired underwater adhesives using amyloids from commercial proteins

Fall 2022 abstracts, posters, and presentations will launch in mid-September.

ACS Fall 2022

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.