title: Modification of hydrophilic and hydrophobic surfaces using an ionic-complementary peptide.
abstract: Ionic-complementary peptides are novel nano-biomaterials with a variety of biomedical applications including potential biosurface engineering. This study presents evidence that a model ionic-complementary peptide EAK16-II is capable of assembling/coating on hydrophilic mica as well as hydrophobic highly ordered pyrolytic graphite (HOPG) surfaces with different nano-patterns. EAK16-II forms randomly oriented nanofibers or nanofiber networks on mica, while ordered nanofibers parallel or oriented 60 degrees or 120 degrees to each other on HOPG, reflecting the crystallographic symmetry of graphite (0001). The density of coated nanofibers on both surfaces can be controlled by adjusting the peptide concentration and the contact time of the peptide solution with the surface. The coated EAK16-II nanofibers alter the wettability of the two surfaces differently: the water contact angle of bare mica surface is measured to be <10 degrees , while it increases to 20.3+/-2.9 degrees upon 2 h modification of the surface using a 29 microM EAK16-II solution. In contrast, the water contact angle decreases significantly from 71.2+/-11.1 degrees to 39.4+/-4.3 degrees after the HOPG surface is coated with a 29 microM peptide solution for 2 h. The stability of the EAK16-II nanofibers on both surfaces is further evaluated by immersing the surface into acidic and basic solutions and analyzing the changes in the nanofiber surface coverage. The EAK16-II nanofibers on mica remain stable in acidic solution but not in alkaline solution, while they are stable on the HOPG surface regardless of the solution pH. This work demonstrates the possibility of using self-assembling peptides for surface modification applications.
authors: Department of Chemical Engineering, University of Waterloo, Waterloo, Ontario, Canada.
authors: Hong
authors: H
authors: Yang
authors: Shan-Yu
authors: SY
authors: Fung
authors: Mark
authors: M
authors: Pritzker
authors: P
authors: P
authors: Chen
mesh_terms: D007477:Ions; D018625:Microscopy, Atomic Force; D049329:Nanostructures; D010455:Peptides / Q000737:chemistry*; D013499:Surface Properties
chemical_list: D007477:Ions; D010455:Peptides