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ARS Home » Northeast Area » Wyndmoor, Pennsylvania » Eastern Regional Research Center » Microbial and Chemical Food Safety » Research » Publications at this Location » Publication #399190
Research Project: Development and Validation of Predictive Models and Pathogen Modeling Programs; and Data Acquisition for International Microbial Databases

Location: Microbial and Chemical Food Safety

Title: Effect of disulfide bonds on the thermal stability of pediocin: In-silico screening using molecular dynamics simulation

Author
item UNAI, MEHMET - Ankara University Of Turkey
item KAYMAZ, OZLEM - Ankara University Of Turkey
item GUNES ALTUNTAS, EVRIM - Ankara University Of Turkey
item Juneja, Vijay
item ELMALI, AYHAN - Ankara University Of Turkey

Submitted to: Journal of Food Protection
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 5/18/2023
Publication Date: 5/23/2023
Citation: Unai, M.A., Kaymaz, O., Gunes Altuntas, E., Juneja, V.K., Elmali, A. 2023. Effect of disulfide bonds on the thermal stability of pediocin: In-silico screening using molecular dynamics simulation. Journal of Food Protection. 86:100107. https://doi.org/10.1016/j.jfp.2023.100107.
DOI: https://doi.org/10.1016/j.jfp.2023.100107

Interpretive Summary: Bacteriocins, Nisin and pediocin, are ribosomally produced peptides produced by lactic acid bacteria and function as natural food preservatives. Since molecular modeling provides a powerful and useful approach for studying protein behavior, we used a computational approach to better understand the antimicrobial activity of pediocin in-silico at different temperatures. This study provided insights into the stability of pediocin at high food processing temperatures and will help the industry to explore new approaches to guard against pathogens in processed foods.

Technical Abstract: The thermal stability properties of pediocin at 310K, 313K, 323K, 333K, 343K, and 348K are reported in this study. A theoretical approach, such as the molecular dynamics method, was used to analyze the structure. Molecular dynamics simulation confirms the stability of molecules with Cys. Furthermore, this study reveals that Cys residues play an essential role in structure stability at high temperatures. To understand the structural basis for the stability of pediocin, a detailed in silico analysis using molecular dynamics simulations to explore the thermal stability profiles of the compounds was conducted. One relevant study found that all pediocin-like bacteriocins have a well-conserved three-stranded antiparallel ß sheet-like structure that is stabilized by a disulfide bond. This study shows that thermal effects fundamentally alter the functionally crucial secondary structure of pediocin. However, as previously reported, pediocin’s activity was strictly conserved due to the disulfide bond between Cys residues. These findings reveal, for the first time, the dominant factor behind the thermodynamic stability of pediocin.