Novel materials from protein-polymer grafts.
Proteins are the most underrated and under-used polymers: their impressive properties include infusibility, great mechanical strength and inherent adhesive capability due to a highly flexible backbone and many functional side chains. The notion of moisture sensitivity of proteins is not universally true. Barnacle cement (which can adhere to Teflon) and mussel and clam byssus, all of which are 99% protein, set in the presence of water and resist enzymatic as well as chemical degradation at ambient temperature. This observation suggests that proteins that are capable of tight three-dimensional cross-linking can overcome sensitivity to moisture and enzymatic attack. It should then be possible to achieve similar resistance by appropriate chemical manipulation of proteins, leading to cross-linking. We have achieved such a result with an ordinary protein, commercially available gelatin, which was chemically modified and then epoxidized. When cured such a material binds to metals and plastics. Any protein that has modifiable amino acids can be used for this purpose.
D000269:Adhesives; D055598:Chemical Phenomena; D002621:Chemistry; D004852:Epoxy Compounds; D005780:Gelatin; D008670:Metals; D010969:Plastics; D011108:Polymers; D011506:Proteins
D000269:Adhesives; D004852:Epoxy Compounds; D008670:Metals; D010969:Plastics; D011108:Polymers; D011506:Proteins; D005780:Gelatin