Analysis of the structure and efficacy of soybean meal antimicrobial peptides

Abstract

In this thesis, soybean meal protein was used to explore its potential in the development of natural antimicrobial peptides. With the increasing problem of antibiotic resistance, the development of safe, efficient and low toxic new antibacterial agents has become a hot research direction. As a by-product of soybean processing, soybean meal is rich in protein, which is a potential source for the preparation of antimicrobial peptides and provides high-quality raw materials for the preparation of bioactive peptides. In this study, the amino acid sequence of β-conglycinin was obtained from the NCBI database, and the peptide fragments were obtained by BIOPEP to simulate the digestion process of pepsin, proteinase K and papain. Then toxicity analysis was performed with ToxinPred to screen out non-toxic peptides. The CAMPR3 and APD3 databases were used to predict the antibacterial and functional properties of the peptides, and the peptides with antibacterial potential such as SCPAASRPGCHKNTCGL, PVWR and APNNMR were screened. Finally, molecular docking experiments using AlphaFold3 showed that the above peptides had a strong binding affinity with the target proteins in E. coli (pTM value >0.88), which verified the antibacterial activity of the peptides. The results showed that there were indeed peptides with good antibacterial activity in soybean meal, and these peptides exhibited low toxicity, high binding affinity and strong predictive antibacterial properties. This study provided a theoretical basis for high-value utilization of soybean meal resources, and also provided a reference for the development and structure optimization of new natural antimicrobial peptides. In the future, its practical efficacy can be further verified by in vitro experiments, and its application prospects in food preservation, animal feed, medicine and other fields can be explored.