Nevertheless, the low synthetic efficiency, high minimum gelation concentrations (MGC), and multiphase composition increased the complexity of nanofibrous polypeptide. Meanwhile, the hydrogels modified or blended with functional polypeptide also enhanced its biological functions. The synthetical polypeptides with nanofibrous structure had been reported to promote cell adhesion and regulate cell behaviors. Hence, it was of great challenge and significance to develop functionally biomimetic polypeptide. However, the complex production processes, expensive manufacturing cost, and immunogenicity due to its animal origin constrained its wide application, ,, ]. It could promote cell adhesion, regulate cellular biofunctions and extracellular matrix formation. Collagen, which is the main component of ECM, consists of three long chains of amino acids spirally twisting in fibrous structure. Recently, more efforts were put on the development of fibrous hydrogels, expecting to acquire highly matched structures and functions with ECMs, , ]. Such biomimetic supramolecular short peptide biomaterials hold great potential in regenerative medicine as promising innovative matrices because of their simple and regular molecular structure and excellent biological performance.įunctional hydrogels had achieved great progress in tissue regeneration since they simulate native extracellular matrix (ECM), ,, ]. These supramolecular nanofiber hydrogels could effectively support chondrocytes spreading and proliferation, and specifically enhance chondrogenic related genes expression and chondrogenic matrix secretion. The storage modulus of BPAA-AFF with 10 nm nanofibers self-assembling was around 13.8 kPa, and the morphology was similar to natural extracellular matrix. Enhanced L929 cells adhesion and proliferation demonstrated good biocompatibility of the hydrogels. The biomechanical properties and intermolecular interactions were also analyzed by rheology and spectroscopy analysis to optimize amino acid sequence.
Using molecular dynamics simulations to interrogate the physicochemical properties of designed biphenyl-tripeptide sequences in atomic detail, reasonable hydrogen bond interactions and “FF” brick (phenylalanine-phenylalanine) promoted the formation of supramolecular fibrous hydrogels. Here, a new class of biphenyl-tripeptides with different C-terminal amino acids sequences transposition were developed, which could self-assemble to form robust supramolecular nanofiber hydrogels from 0.7 to 13.8 kPa at ultra-low weight percent (about 0.27 wt%). Supramolecular nanofiber peptide assemblies had been used to construct functional hydrogel biomaterials and achieved great progress.
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