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 …

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

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

Elastin-derived peptides are gaining increasing interest as potential biomaterials. Previous
studies have demonstrated that short elastin-derived peptides are able to self-assemble into …

Tropoelastin is the primary component of elastin, which forms the elastic fibers that make up
connective tissues. The hydrophobic domains of tropoelastin are thought to mediate the self …

Well‐defined tunable nanostructures formed through the hierarchical self‐assembly of
peptide building blocks have drawn significant attention due to their potential applications in …

Inspired by self-assembling peptides found in native proteins, deliberately designed
engineered peptides have shown outstanding biocompatibility, biodegradability, and …

Elastin‐like polypeptides (ELPs) are biopolymers composed of short repeating peptide
motifs inspired by the native elastin hydrophobic domains, mostly the pentapeptide VPGXG …

Elastin-like polypeptides (ELPs) are a class of biopolymers consisting of the pentameric
repeat (VPGαG) n based on the sequence of mammalian tropoelastin that display a …

Large protein‐based micellar aggregates (see Figure) are reversibly formed upon self‐
assembly of the amphiphilic diblock copolymer—based on elastin‐mimetic peptide …