Self-Assembly of Elastin–Mimetic Double Hydrophobic Polypeptides
journal contributionposted on 08.04.2013 by Duc H. T. Le, Ryo Hanamura, Dieu-Huong Pham, Masaru Kato, David A. Tirrell, Tatsuya Okubo, Ayae Sugawara-Narutaki
Any type of content formally published in an academic journal, usually following a peer-review process.
We have constructed a novel class of “double-hydrophobic” block polypeptides based on the hydrophobic domains found in native elastin, an extracellular matrix protein responsible for the elasticity and resilience of tissues. The block polypeptides comprise proline-rich poly(VPGXG) and glycine-rich poly(VGGVG), both of which dehydrate at higher temperature but form distinct secondary structures, β-turn and β-sheet respectively. In water at 45 °C, the block polypeptides initially assemble into nanoparticles rich in β-turn structures, which further connect into long (>10 μm), beaded nanofibers along with the increase in the β-sheet content. The nanofibers obtained are well-dispersed in water, and show thermoresponsive properties. Polypeptides comprising each block component assemble into different morphologies, showing that the conjugation of poly(VPGXG) and poly(VGGVG) plays a role for beaded fiber formation. These results may provide innovative ideas for designing peptide-based materials but also opportunities for developing novel materials useful for tissue engineering and drug delivery systems.