Genetic engineering of protein-based materials provides material scientists with high levels of control in material microstructures, properties, and functions [1]. For example, multi-block protein copolymers in which individual block may possess distinct mechanical or biological properties have been biosynthesized [2, 3]. Polypeptide sequences derived from well-studied structural proteins (e.g., collagen, silk, elastin) are often used as motifs in the design and synthesis of new protein-based material, in which new functional groups may be incorporated. In this fashion, we have produced a series of silk-elastin-like proteins (SELPs) consisting of polypeptide sequences derived from silk of superior mechanical strength and elastin that is extremely durable and resilient [2, 4]. Notably, the silk-like blocks are capable of crystallizing to form virtual cross-links between elastin-mimetic sequences, which, in turn, lower the crystallinity of the silk-like blocks and thus enhance the solubility of SELPs. Consequently, SELPs may be fabricated into useful structures for biomedical applications, including drug delivery. In this study, we will characterize viscoelastic properties of SELPs, which are particularly relevant to tissue engineering applications.
Rational Design and Synthesis of Right-Handed d-Sulfono-γ-AApeptide Helical Foldamers as Potent Inhibitors of Protein–Protein Interactions
