Record Details
Molecular origins of peptide entrapment in polyethylene oxide layers
ScholarsArchive at Oregon State University
| Field | Value |
|---|---|
| Title | Molecular origins of peptide entrapment in polyethylene oxide layers |
| Names |
Wu, Xiangming
(creator) McGuire, Joseph (advisor) Schilke, Karl F. (advisor) |
| Date Issued | 2014-02-26 (iso8601) |
| Note | Graduation date: 2014 |
| Abstract | A more quantitative understanding of peptide entrapment and elution from otherwise protein-repellent polyethylene oxide (PEO) brush layers will provide direction for development of new strategies for drug storage and delivery. Here we describe criteria for peptide integration and structural change within the PEO brush, and discuss the reversibility of peptide entrapment with changing solvent conditions. For this purpose, three cationic peptides were used: the arginine-rich amphiphilic peptide WLBU2, the chemically identical but scrambled peptide S-WLBU2, and the non-amphiphilic homopolymer poly-L-arginine (PLR). Circular dichroism (CD) was used to record the adsorption and conformational changes of (amphiphilic) WLBU2 and S-WLBU2, and (non-amphiphilic) polyarginine peptides, at uncoated (hydrophobic) and PEO-coated silica nanoparticles. UV spectroscopy and a quartz crystal microbalance with dissipation monitoring (QCM-D) were used to quantify changes in the extent of peptide elution. Peptide conformation was controlled between disordered and α-helical forms by varying the concentration of perchlorate ion. We show an initially more ordered (α-helical) structure promotes peptide adsorption into the PEO layer. Further, a partially helical peptide undergoes an increase in helicity after entry, likely due to concomitant loss of capacity for peptide-solvent hydrogen bonding. Peptide interaction with the PEO chains resulted in entrapment and conformational change that was irreversible to elution with changing solution conditions in the case of the amphiphilic peptide. In contrast, the adsorption and conformational change of the non-amphiphilic peptide was reversible. We also evaluated the effects of peptide surface density on the conformational changes caused by peptide-peptide interactions, and using CD, QCM-D, and UV spectroscopy, showed that these phenomena substantially affect the rate and extent of peptide elution from PEO brush layers. Specifically, for amphiphilic peptides at sufficiently high surface density, peptide-peptide interactions result in conformational changes which compromise their resistance to elution. In contrast, elution of a non-amphiphilic peptide is substantially independent of its surface density, presumably due to the absence of peptide-peptide interactions. The sequential and competitive adsorption behavior of WLBU2, S-WLBU2 and PLR at pendant PEO layers was studied by optical waveguide lightmode spectroscopy (OWLS), time-of-flight secondary ion mass spectrometry (TOF-SIMS), CD and UV spectroscopy. Results strongly indicate that amphiphilic peptides are able to displace non-amphiphilic peptides that are adsorbed in PEO layers, while non-amphiphilic peptides cannot displace amphiphilic ones. In summary, peptides of high amphiphilicity are expected to dominate the competitive adsorption with less amphiphilic peptides in PEO layers. |
| Genre | Thesis/Dissertation |
| Access Condition | http://creativecommons.org/licenses/by-nd/3.0/us/ |
| Topic | peptide adsorption |
| Identifier | http://hdl.handle.net/1957/46570 |
