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Biomacromolecules. 2013 Apr 8;14(4):1028-34. doi: 10.1021/bm301887m. Epub 2013 Mar 28.

Self-assembly of elastin-mimetic double hydrophobic polypeptides.

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1
Department of Chemical System Engineering, The University of Tokyo, 7-3-1 Hongo, Tokyo 113-8656, Japan.

Abstract

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.

PMID:
23495825
DOI:
10.1021/bm301887m
[Indexed for MEDLINE]
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