Controlling Interfacial Adhesion of Self-Assembled Polypeptide Fibrils for Novel Nanoelectromechanical System (NEMS) Applications

The relative adhesion of two genetically engineered polypeptides termed as H6-(YEHK)x21-H6 and C6-(YEHK)X21-H6 has been investigated following growth and self-assembly on highly oriented pyrolytic graphite (HOPG), SiO2, Ni, and Au substrates to study covalent surface attachment via histidine (H) and cysteine (C) groups incorporated in the polypeptides. Both polypeptides formed predominantly bilayer fibrils upon deposition, in agreement with previous studies. The relative adhesion of polypeptide fibrils to the substrate, as well as intra-fibril cohesion, was examined via a forced-scanning method employing contact mode atomic force microscopy (AFM). H6-(YEHK)x21-H6 polypeptide fibrils were observed to detach from Ni, Au, SiO2, and HOPG substrates at normal tip forces of 106 ± 10 nN, 21 ± 3 nN, 22 ± 3 nN, and 3 ± 1 nN, respectively. C6-(YEHK)x21-H6 polypeptide fibrils were seen to detach from Au substrates at a normal spring force of 90 ± 10 nN. It is concluded that the H6-(YEHK)x21-H6 and C6-(YEHK)x21-H6 polypeptide fibrils are covalently attached to, respectively, Ni and Au substrates, which has important implications for the use of these materials for NEMS fabrication. The structural stability of deposited polypeptide fibrils was also evaluated by using normal tip forces less than those required for fibril detachment. H6-(YEHK)x21-H6 polypeptide fibrils on Ni substrates were the most structurally stable compared to C6-(YEHK)x21-H6 polypeptide fibrils on Au substrates. Controlled delayering of bilayer fibrils was also detected for sub-detachment normal forces. OPEN ACCESS Micromachines 2011, 2 2