Self-Assembly of Elastin–Mimetic Double Hydrophobic Polypeptides Duc H. T. Le Ryo Hanamura Dieu-Huong Pham Masaru Kato David A. Tirrell Tatsuya Okubo Ayae Sugawara-Narutaki 10.1021/bm301887m.s001 https://acs.figshare.com/articles/journal_contribution/Self_Assembly_of_Elastin_Mimetic_Double_Hydrophobic_Polypeptides/2426146 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. 2013-04-08 00:00:00 tissue show thermoresponsive properties material nanofiber extracellular matrix protein drug delivery systems block polypeptides