Surface and adsorption characteristics of three elastin-like polypeptide coatings with varying sequence lengths.

The surface properties of a family of elastin-like polypeptides (ELPs), differing in molecular weight and sequence length, were investigated to understand how the nature of the polypeptide film might contribute to their thrombogenic profile. Physical adsorption of the ELPs onto Mylar increased surface wettability as the sequence length decreased while X-ray spectroscopy analysis showed an increasing amide content with sequence length. Chemical force microscopy analysis revealed that the ELP-coated surfaces displayed purely hydrophilic adhesion forces that increased as the ELP sequence length decreased. Adsorption isotherms performed using the quartz crystal microbalance with dissipation, showed that the surface coverage increased with ELP sequence length. The longer polypeptides (ELP2 and ELP4) also displayed higher specific dissipation values indicating that they established films with greater structural flexibility and associated water content than the shorter polypeptide, ELP1. Additionally, the stability of the ELP coating was lower with the shorter polypeptides. This study highlights the different surface properties of the ELP coatings as well as the dynamic nature of the ELP adsorbed layer wherein the conformational state may be an important factor contributing to their blood response.