POLY 164 |
| Traditionally, hydrogel materials that swell or contract with changes in temperature are termed thermally responsive. Self-assembly strategies using β-hairpin peptides provide precise control in order to construct new hydrogel materials that can be responsive to temperature. In this work, thermally responsive beta-hairpin peptides were designed using hydrophilic and hydrophobic amino acids. These peptides have two extended sequences contain alternating hydrophilic and hydrophobic residues, at the N and C-terminals of a VDPPT tetrapeptide. Lysine (K) occupies the hydrophilic positions, while valine (V), a residue of high β-sheet propensity, is used as the primary hydrophobic residue. We investigated the stability of these peptides in several solvents, and evaluated correlation between thermal behavior and molecular interaction by measuring CD spectra.
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General Papers: Functional Materials
6:00 PM-8:00 PM, Sunday, August 19, 2007 BCEC -- Exhibit Hall - B2, Poster
Division of Polymer Chemistry |