Abstract How to improve the activity of antioxidant peptides had become a research hotspot in biomedical field in recent years. In this paper, we explore self-assembly used as a new… Click to show full abstract
Abstract How to improve the activity of antioxidant peptides had become a research hotspot in biomedical field in recent years. In this paper, we explore self-assembly used as a new method to enhance the antioxidant activity of peptides. Separate peptide VLLY and KDHCH were selected and assembled the polypeptide VLLYKDHCH. Firstly, the DPPH radical scavenging of VLLYKDHCH was 74.57% higher than that of VLLY and 71.26% higher than that of KDHCH at the concentration of 3mmoL/ml. Therefore, we inferred the self-assembly of peptides affect the antioxidant capacity of polypeptide. Furthermore, we investigate the improvement mechanism by means of circular dichroism (CD), and the prediction confirmed by the molecular dynamics (MD) simulation, Raman spectrum and the 1H NMR spectrum. The random crimp degree of the secondary structure increased after two different proteins were bound together. The assembled secondary structure and self-assembly behavior of the three isolated peptides in aqueous solution was demonstrated by continuous experiments.
               
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