Abstract

Polymers are widely used for many applications ranging from biomedical materials, marine antifouling coatings, membranes for biomolecule separation, to substrates for enzyme molecules for biosensing. For such applications, it is important to understand molecular interactions between biological molecules and polymer materials in situ in real time. Such understanding provides vital knowledge to manipulate biological molecule-polymer interactions and to optimize polymer surface structures to improve polymer performance. In this research, sum frequency generation (SFG) vibrational spectroscopy was applied to study interactions between peptides (serving as models for biological molecules) and deuterated polystyrene (d8-PS, serving as a model for polymer materials). The peptide conformations/orientations and polymer surface phenyl orientation during the peptide-d8-PS interactions were determined using SFG. It was found that the π-π interaction between the aromatic amino acids on peptides and phenyl groups on d8-PS surface does not play a significant role. Instead, the peptide-d8-PS interactions are mediated by general hydrophobic interactions between the peptides and the polymer surface.

Full Text
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