Surface Structure and Hydration of Sequence-Specific Amphiphilic Polypeptoids for Antifouling/Fouling Release Applications.

Amphiphilic polypeptoids can be designed with specific sequences of hydrophilic and hydrophobic units, which determine their surface properties for antifouling/fouling release purposes. Although the sequence-dependent surface structures of polypeptoids have been extensively investigated, e.g., with X-ray spectroscopy, their molecular structures under the aqueous conditions relevant to marine fouling have not been studied. In this work, we applied sum frequency generation (SFG) vibrational spectroscopy to study the surface structures and hydration of a series of amphiphilic polypeptoid coatings with different sequences in air and water. SFG spectra, in agreement with X-ray spectroscopy studies, revealed that the surface coverage of the hydrophilic N-(2-methoxyethyl)glycine (Nme) units in air is affected by both the number and position of the hydrophobic N-(heptafluorobutyl)glycine (NF) units in the peptoid chain and is negatively correlated with the surface concentration of the fluorine element. Our ability to probe the SFG signals of water molecules at the peptoid surface provides new information on the hydrated film properties. From these SFG signals and the time evolution of water contact angles on the polymers, we see that the hydrated film properties are also dependent upon the peptoid sequence. This work indicates that the surface presence of the Nme groups and the ability of the polymers to order and strongly hydrogen bond with interfacial water molecules determine their antifouling properties, whereas the surface restructuring rate upon contact with water affects their fouling release behaviors.