We have recently developed a novel double‐hydrophobic elastin‐like triblock polypeptide
called GPG, designed after the uneven distribution of two different hydrophobic domains …

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 …

Abstract A “double‐hydrophobic” elastin‐like triblock polypeptide GPG has been constructed
by mimicking the localization of proline‐and glycine‐rich hydrophobic domains of native …

Elastin-like polypeptides (ELPs) are promising candidates for fabricating tissue-engineering
scaffolds that mimic the extracellular environment of elastic tissues. We have developed a …

Elastin polypeptides based on-VPGVG-repeated motifs are widely used in the production of
biomaterials because they are stimuli-responsive systems. On the other hand, glycine-rich …

A double hydrophobic elastin-like block polypeptide having crosslinkable amino groups at
both termini has been constructed for the first time. Upon an increase in temperature, the …

A small library of short peptides has been synthesized based upon the repeat tetrapeptide
sequence Gly‐Val‐Ala‐Pro (GVAP) which is found in the hydrophobic domain of …

In biomedical applications, there is a need for tissue engineering scaffolds to promote and
control cellular behaviors, including adhesion, proliferation and differentiation. In particular …

Protein polymers derived from elastin-mimetic peptide sequences can be synthesized with
near-absolute control of macromolecular architecture using genetic engineering techniques …

Novel thermo-responsive elastin-like oligopeptides containing cell-binding epitope (Arg-Gly-
Asp-Ser sequence); arginine-glycine-aspartic acid-serine (RGDS)-elastin-like peptides …