Self-Assembly of Elastin–Mimetic Double Hydrophobic Polypeptides

• Published in: Biomacromolecules 2013-04, Vol.14 (4), p.1028-1034
• Main Authors: Le, Duc H. T, Hanamura, Ryo, Pham, Dieu-Huong, Kato, Masaru, Tirrell, David A, Okubo, Tatsuya, Sugawara-Narutaki, Ayae
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Aminoacid polymers; Analytical, structural and metabolic biochemistry; Applied sciences; Biological and medical sciences; Biomimetics; Drug Delivery Systems; Elastin - chemistry; Exact sciences and technology; Fundamental and applied biological sciences. Psychology; Hydrophobic and Hydrophilic Interactions; Miscellaneous; Nanofibers; Nanoparticles; Peptides - chemistry; Physicochemistry of polymers; Protein Structure, Secondary; Proteins; Synthetic biopolymers; Tissue Engineering
• ISSN: 1525-7797; 1526-4602
• DOI: 10.1021/bm301887m

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.