Molecular origins of peptide entrapment within polyethylene oxide brush layers Public

http://ir.library.oregonstate.edu/concern/honors_college_theses/02870x85t

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  • Effective surface coatings for tissue-contacting medical devices should prevent both biofilm formation and infection. One method to achieve this aim is protein repellant polyethylene oxide (PEO) brush coatings loaded with antimicrobials. Previous research has demonstrated that the antimicrobial nisin adsorbs to PEO brush layers in multi-layer amounts and suggests that small peptides or proteins are capable of being loaded into an otherwise protein repellent brush. The work described in this thesis aimed to understand the influences of peptide structure and amphiphilicity on adsorption into brush layers and is a necessary step in the development of bioactive coatings. Optical waveguide lightmode spectroscopy was used to investigate the adsorption of polyglutamic acid and the cationic amphiphilic peptide WLBU2 to a PEO brush. Kinetic parameters were interpreted with respect to a model accounting for history-dependent adsorption, in order to evaluate rate constants for peptide adsorption and desorption, as well as the lateral clustering behavior of an absorbed or entrapped peptide. The WLBU2 peptide was held within the brush even after sustained rinsing, whereas the desorption data suggested that polyglutamic acid would completely elute from the brush with time. These results indicate that small peptides are capable of becoming entrapped within PEO brushes and that amphiphilic peptides are held more tightly. The results presented here are compelling evidence of the potential to create anti-fouling surface coatings capable of storing and delivering therapeutics.
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