4 research outputs found
Self-Assembly of Elastin–Mimetic Double Hydrophobic Polypeptides
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
Self-Assembly of Elastin–Mimetic Double Hydrophobic Polypeptides
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
polyÂ(VPGXG) and glycine-rich polyÂ(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 ÎĽm), 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 polyÂ(VPGXG)
and polyÂ(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