Effect of Disulfide Bonds on the Thermal Stability of Pediocin: In-silico Screening Using Molecular Dynamics Simulation

Ünal, Mehmet Altay; Kaymaz, Özlem; Altuntaş, Evrim Güneş; Juneja, Vijay K.; Elmalı, Ayhan

doi:10.1016/j.jfp.2023.100107

Cited by 3 publications

(1 citation statement)

References 38 publications

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“…Some class IIa bacteriocins, such as sakacin G, plantaricin 423, pediocin PA-1/AcH, divercin V41 and enterocin A, have an extra disulphide bond in the C-terminal [ 38 ]. Studies have shown that bacteriocins containing two disulphide bonds may have higher antimicrobial potency and thermal stability [ 38 , 39 ].…”

Section: General Properties Of Class Iia Bacteriocinsmentioning

confidence: 99%

The Progress of the Biotechnological Production of Class IIa Bacteriocins in Various Cell Factories and Its Future Challenges

Wang,

Shang,

Huang

et al. 2024

IJMS

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Class IIa bacteriocins produced in lactic acid bacteria are short cationic peptides with antimicrobial activity. In the search for new biopreservation agents, class IIa bacteriocins are considered to be the best potential candidates, not only due to their large abundance but also because of their high biological activity and excellent thermal stability. However, regulated by the biosynthetic regulatory system, the natural class IIa bacteriocin yield is low, and the extraction process is complicated. The biotechnological production of class IIa bacteriocins in various cell factories has been attempted to improve this situation. In this review, we focus on the application of biotechnological routes for class IIa bacteriocin production. The drawbacks and improvements in the production of class IIa bacteriocins in various cell factories are discussed. Furthermore, we present the main challenge of class IIa bacteriocins, focusing on increasing their production by constructing suitable cell factories. Recombinant bacteriocins have made considerable progress from inclusion body formation, dissolved form and low antibacterial activity to yield recovery. The development of prospective cell factories for the biotechnological production of bacteriocins is still required, which may facilitate the application of bacteriocins in the food industry.

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Section: General Properties Of Class Iia Bacteriocinsmentioning

confidence: 99%

The Progress of the Biotechnological Production of Class IIa Bacteriocins in Various Cell Factories and Its Future Challenges

Wang,

Shang,

Huang

et al. 2024

IJMS

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Molecular Dynamic Study on the Structure and Thermal Stability of Mutant Pediocin PA-1 Peptides Engineered with Cysteine Substitutions

SEVİM,

GÜNEŞ ALTUNTAŞ

2024

Probiotics & Antimicro. Prot.

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Pediocin and analogous bacteriocins, valued for thermal stability, serve as versatile antimicrobials in the food sector. Improving their resilience at high temperatures and deriving derivatives not only benefit food production but also offer broad-spectrum antimicrobial potential in pharmaceuticals, spanning treatments for peptic ulcers, women’s health, and novel anticancer agents. The study aims to create mutant peptides capable of establishing a third disulfide bond or enhanced through cysteine substitutions. This involves introducing additional Cys residues into the inherent structure of pediocin PA-1 to facilitate disulfide bond formation. Five mutants (Mut 1–5) were systematically generated with double Cys substitutions and assessed for thermal stability through MD simulations across temperatures (298–394 K). The most robust mutants (Mut 1, Mut 4–5) underwent extended analysis via MD simulations, comparing their structural stability, secondary structure, and surface accessibility to the reference Pediocin PA-1 molecule. This comprehensive assessment aims to understand how Cys substitutions influence disulfide bonds and the overall thermal stability of the mutant peptides. In silico analysis indicated that Mut 1 and Mut 5, along with the reference structure, lose their helical structure and one natural disulfide bond at high temperatures, and may impacting antimicrobial activity. Conversely, Mut 4 retained its helical structure and exhibited thermal stability similar to Pediocin PA-1. Pending further experimental validation, this study implies Mut 4 may have high stability and exceptional resistance to high temperatures, potentially serving as an effective antimicrobial alternative.

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Solubility, thermodynamic investigation and molecular dynamics simulation of guanidine hydrochloride in four binary solvents

He,

Guo,

Wan

et al. 2023

Journal of Molecular Liquids

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Effect of Disulfide Bonds on the Thermal Stability of Pediocin: In-silico Screening Using Molecular Dynamics Simulation

Cited by 3 publications

References 38 publications

The Progress of the Biotechnological Production of Class IIa Bacteriocins in Various Cell Factories and Its Future Challenges

The Progress of the Biotechnological Production of Class IIa Bacteriocins in Various Cell Factories and Its Future Challenges

Molecular Dynamic Study on the Structure and Thermal Stability of Mutant Pediocin PA-1 Peptides Engineered with Cysteine Substitutions

Solubility, thermodynamic investigation and molecular dynamics simulation of guanidine hydrochloride in four binary solvents

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