title: [Study on the self-assembly and cytocompatibility of the natural amino acid biomaterials].
abstract: Functional designing of natural amino acids (NAA) has received considerable attention in recent years due to its excellent biocompatibility. A novel self-assembling NAA, peptide RAG-16, was designed by hybridizing the characteristic silk fibroin motif (Gly-Ala) with an ionic complementary peptide sequence (Arg-Ala-Asp-Ala) in our study. The self-assembly structure, viscoelastic property, and cyto compatibility of the peptide were investigated by atomic force microscopy, rheometer, Fourier transform infrared spectrum, and inverted fluorescence microscope. RAG-16 was able to form a three-dimensional compact network structure in water. High mechanical performance of the peptide hydrogel was found due to the increase of the silk I structure from inserted fibroin motif segment. Fluorescence staining showed that vast majority of MC3T3-E1 cells in the RAG-16 hydrogel could adhere to, survive, and distribute on different planes. To sum up, in this experiment, the functional designing of the NAA has exhibited its potential application in biomedical field.
authors.affiliation: College of Chemical & Environment Protection, Southwest University for Nationalities, Chengdu 610041, China.
authors.forename: Qinghan
authors.initials: Q
authors.lastname: Zhou
authors.forename: Juan
authors.initials: J
authors.lastname: Lin
mesh_terms: D000596:Amino Acids / Q000737:chemistry*; D001672:Biocompatible Materials / Q000737:chemistry*; D005349:Fibroins / Q000737:chemistry; D020100:Hydrogels / Q000737:chemistry; D008958:Models, Molecular; D049329:Nanostructures / Q000737:chemistry* / Q000648:ultrastructure*; D010455:Peptides / Q000737:chemistry*; D047011:Silk / Q000737:chemistry
chemical_list: D000596:Amino Acids; D001672:Biocompatible Materials; D020100:Hydrogels; D010455:Peptides; D047011:Silk; D005349:Fibroins