Deciphering anti-biofilm property of Arthrospira platensis-origin peptides against Staphylococcus aureus

Arthrospira platensis is a valuable natural health supplement consisting of various types of vitamins, dietary minerals, and antioxidants. Although different studies have been conducted to explore the hidden benefits of this bacterium, its antimicrobial property has been poorly understood. To decipher this important feature, here, we extended our recently introduced optimization algorithm (Trader) for aligning amino acid sequences associated with the antimicrobial peptides (AMPs) of Staphylococcus aureus and A. platensis. As a result, similar amino acid sequences were identified, and several candidate peptides were generated accordingly. The obtained peptides were then filtered based on their potential biochemical and biophysical properties, and their 3D structures were simulated based on homology modeling techniques. Next, to investigate how the generated peptides can interact with S. aureus proteins (i.e., heptameric state of the hly and homodimeric form of the arsB), molecular docking approaches were used. The results indicated that four peptides included better molecular interactions relative to the other generated ones in terms of the number/average length of hydrogen bonds and hydrophobic in-teractions. Based on the outcomes, it can be concluded that the antimicrobial property of A. platensis might be associated with its capability in disturbing the membrane of pathogens and their functions.

Automated summary

In this study, an optimization algorithm (Trader) was used to align amino acid sequences associated with antimicrobial peptides (AMPs) of Staphylococcus aureus and Arthrospira platensis. Similar sequences were identified, and candidate peptides were generated and filtered based on biochemical and biophysical properties. The 3D structures of the peptides were simulated using homology modeling techniques. Molecular docking approaches were then used to investigate the interactions between the generated peptides and S. aureus proteins. Results showed that four peptides had better molecular interactions, suggesting that the antimicrobial property of A. platensis may be attributed to its ability to disrupt the membrane and functions of pathogens.