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