| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 6983583 | Colloids and Surfaces B: Biointerfaces | 2013 | 7 Pages |
Abstract
- α-Helical peptides penetrate PEO brushes, while “disordered” conformations do not.
- Peptide α-helicity increases in the hydrophobic inner region within a PEO brush.
- The elutability of non-amphiphilic peptides depends on bulk solution conditions.
- Amphiphilic peptides are resistant to elution, regardless of solution conditions.
- Structure-based peptide-PEO associations may enable novel drug delivery strategies.
Keywords
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Colloid and Surface Chemistry
Authors
Xiangming Wu, Matthew P. Ryder, Joseph McGuire, Karl F. Schilke,