(360a) All-in-One Peptide Biomaterial: Biomolecular Recognition, Ultra-Low Fouling, and Surface Anchoring

Proteins in the human body are able to avoid nonspecific adsorption and are stable in complex media. These are two desirable properties for many biomedical applications including biosensors, drug delivery, and tissue engineering. By examining the surfaces of proteins we can seek inspiration for new stealth materials that are biocompatible. The analysis of over a thousand proteins indicates that glutamic acid (E) and lysine (K) are the two most prevalent amino acids on the surfaces of proteins. Based on this knowledge, a nonfouling peptide was rationally designed by alternating negatively charged E and positively charged K amino acid residues. A linker of four residues in length (-PPPPC) and of a rigid, hydrophobic nature was included to form a well-ordered structure and high surface density coating onto a gold surface. Finally, the peptide sequence EKEKEKE-PPPPC-Am was extended with the cell-binding sequence RGD to demonstrate control over specific vs. nonspecific cell adhesion without using synthetic polymers such as poly (ethylene) glycol (PEG). The combination of peptide sequences with different properties allows for a versatile platform combining several functions in one material. This talk will identify key design principles for peptide-based low fouling materials inspired by native proteins. In addition, the rational design of the peptide sequence to achieve a robust surface coating and the characterization of these surfaces for nonspecific protein adsorption, secondary structure, surface anchoring, and specific cell adhesion will be presented.