TY - DATA T1 - Self-Assembly of Elastin–Mimetic Double Hydrophobic Polypeptides PY - 2013/04/08 AU - Duc H. T. Le AU - Ryo Hanamura AU - Dieu-Huong Pham AU - Masaru Kato AU - David A. Tirrell AU - Tatsuya Okubo AU - Ayae Sugawara-Narutaki UR - https://acs.figshare.com/articles/journal_contribution/Self_Assembly_of_Elastin_Mimetic_Double_Hydrophobic_Polypeptides/2426146 DO - 10.1021/bm301887m.s001 L4 - https://ndownloader.figshare.com/files/4067935 KW - tissue KW - show thermoresponsive properties KW - material KW - nanofiber KW - extracellular matrix protein KW - drug delivery systems KW - block polypeptides N2 - 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. ER -