The effect of putrescine on the lysozyme activity and structure: Spectroscopic approaches and molecular dynamic simulation

Ashrafi, Narges; Shareghi, Behzad; Farhadian, Sadegh; Hosseini-Koupaei, Mansoore

doi:10.1016/j.colsurfb.2022.112402

Cited by 7 publications

(2 citation statements)

References 67 publications

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“…Additionally, the Root-Mean-Square Fluctuation (RMSF) is beneficial for illustrating conformational changes in the protein and polypeptide chain. [54,55] The RMSF of the backbone atoms of each residue in the LYS-TFA complex and free LYS is calculated to reveal the flexibility of the backbone structure. The RMSF of the residues is shown in Figure 7b, which clearly shows different flexibility in LYS in the absence and presence of TFA.…”

Section: Molecular Dynamics Studymentioning

confidence: 99%

Molecular Interactions between a Flavonoid and Lysozyme: A Spectroscopic, Thermodynamic, and Computational Study

Mandal

2023

ChemistrySelect

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Transferulic acid has therapeutic importance hence it is very crucial to understand how this molecule interacts with lysozyme proteins for the purpose of drug design, and evaluation. The study is very helpful for drug pharmacology and the thermodynamic parameters of the polyphenolic compound and this protein interaction which is important for disease encounter and prevention. Here the spectroscopic, thermodynamic, and computational study has been reported as experiments. The CD study of the binding of lysozyme and trans ferulic acid found significant structural stability of the protein. Spectroscopically the UV‐Vis & fluorescence study has shown a substantial shift of absorption spectra in the binding of these two molecules, to confirm the interaction. An ITC experimental study found an affinity of the molecule to protein with a binding constant of Ka having a significant value. The Molecular Dynamics study found details of the geometric posture and main force of binding of TFA molecule upon binding with lysozyme site in PBS buffer at physiological pH value. The complex of lysozyme and trans ferulic acid also proved as a stable conformation by Molecular Dynamics study. In the DSC study, stable interaction of lysozyme and trans ferulic acid is shown upon changing the melting enthalpies and temperatures.

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Section: Molecular Dynamics Studymentioning

confidence: 99%

Molecular Interactions between a Flavonoid and Lysozyme: A Spectroscopic, Thermodynamic, and Computational Study

Mandal

2023

ChemistrySelect

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“…At the alkaline pH, all acidic side chains of lysozyme ionized either in native or unfolded states. While at low pH such as 1.5, all the basic chains of lysozyme are fully protonated in both native and unfolded states; and in the pH range of 1.5-5, several groups of lysozyme would be protonated (Ashrafi et al, 2022;Attri et al, 2021).…”

Section: Effect Of Temperaturementioning

confidence: 99%

Secondary Structural Conformation of Lysozyme at Lipid Membrane Interface Using Circular Dichroism Spectroscopy

Majid¹,

Naz²,

Laghari³

et al. 2022

JIS

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A range of experimental techniques have been published to investigate the processes of folding and unfolding of proteins, most of them are relying on a spectroscopic analysis), such as circular Dichroism, tryptophan fluorescence, and a specific denaturation method in which protein folding and unfolding Abstract | This study employs the Circular Dichroism Spectroscopy (CDS) to unfold the possible changes in secondary structural conformation of lysozymes in different pH, temperature and lipid bilayer interfaces. The choice of solvents for the proteins functionality is remained a challenge for biochemical applications, hence there is always a need to understand the effects of solvents on secondary structural conformation. Biophysical investigations about the changes in secondary structure conformation of lysozymes were performed with CDS using them in water and buffer. Membrane bilayer mimics were prepared from dimyristoylphosphatidylcholine (DMPC) through rehydration method. CDS identified that secondary structure was maintained in saline phosphate buffer (PBS) pH (6.4, 7.4 and 8.0), similar to that of water. Temperature based experiments depicted the resistance due to changes in the secondary structural conformation up to 50 °C, however such resistance was reversible after the cooling to 20 °C. In both solvents (PBS and water) lysozyme was predominantly folded to α-helical conformation. At 50 °C, helices were altered to turns. However, in presence of dimyristoylphosphatidylcholine (DMPC) lipid bilayer interfaces, lysozyme adopted β-sheet conformation. This study proposed that hydrophobic groves of lysozyme could be a key in changes of structural conformation while interacting with lipid membrane bilayers. Such protein membrane interactions would facilitate the membrane perturbation. Here, we confirmed the supporting evidence that lysozyme could perturb the lipid bilayer and conforming the sheet structure. Overall, this research suggests that lysozyme could be a tool for designing the novel drug delivery vehicles along its already published potential application.

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Effects of the molecular weight of hyaluronan on the conformation and release kinetics of self-assembled 5-fluorouracil-loaded lysozyme-hyaluronan colloidal nanoparticles

Liu

Wei

et al. 2022

International Journal of Biological Macromolecules

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The effect of putrescine on the lysozyme activity and structure: Spectroscopic approaches and molecular dynamic simulation

Cited by 7 publications

References 67 publications

Molecular Interactions between a Flavonoid and Lysozyme: A Spectroscopic, Thermodynamic, and Computational Study

Molecular Interactions between a Flavonoid and Lysozyme: A Spectroscopic, Thermodynamic, and Computational Study

Secondary Structural Conformation of Lysozyme at Lipid Membrane Interface Using Circular Dichroism Spectroscopy

Effects of the molecular weight of hyaluronan on the conformation and release kinetics of self-assembled 5-fluorouracil-loaded lysozyme-hyaluronan colloidal nanoparticles

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