Amyloid fibrils belong to a category of abnormal aggregations of natural proteins, which are closely related to many human diseases. Recently, some critical peptide sequences have been extensively studied for clarifying the molecular mechanism of natural proteins to form amyloid fibrils. In the present study, we designed a short peptide GGAAVV (GAV-6) composed of hydrophobic amino acids glycine (G), alanine (A) and valine (V) and studied its ability to form amyloid fibrils. As characterized by atomic force microscopy (AFM) and dynamic light scattering (DLS), the peptide could self-assemble into smooth nanofibers without branches. Congo red staining/binding and thioflavin-T (ThT) binding experiments show that the nanofibers formed by GAV-6 shared identical properties with typical amyloid fibrils. These results show that the designed peptide GAV-6 could self-assemble into typical amyloid fibrils, which might make it a useful model molecule to clarify the mechanism for the formation of amyloid fibrils in the future.
ObjectiveTo review the biological characteristics of self-assembling peptide nanofiber scaffold (SAPNS) and its potential to induce bone repair. MethodsThe literature regarding SAPNS and its application in bone repair was extensively analyzed and reviewed. ResultsSAPNS is derived from natural amino acids, and has the properties of good biocompatibility and non-toxic degradation products. Their microenvironment highly mimics the natural extracellular matrix, and controlled release of growth factors as well as modification with functional motifs can substantially improve their bioactivity. Many studies on cell composite culture and bone defect repair of animal models reveal that SAPNS has the ability to promote the function of bone cells (e.g. adherence, proliferation, and differentiation) in vitro, and enhance new bone tissue formation in vivo. ConclusionSAPNS may be an ideal material for bone repair, but its biologically mechanical properties need further improvement.