Study on the self-assembly and cytocompatibility of the natural amino acid biomaterials.
- Author:
Qinghan ZHOU
1
;
Juan LIN
Author Information
1. College of Chemical & Environment Protection, Southwest University for Nationalities, Chengdu 610041, China.
- Publication Type:Journal Article
- MeSH:
Amino Acids;
chemistry;
Biocompatible Materials;
chemistry;
Fibroins;
chemistry;
Hydrogels;
chemistry;
Models, Molecular;
Nanostructures;
chemistry;
ultrastructure;
Peptides;
chemistry;
Silk;
chemistry
- From:
Journal of Biomedical Engineering
2012;29(5):898-902
- CountryChina
- Language:Chinese
-
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.
