Investigation on the interaction of cefpirome sulfate with lysozyme by fluorescence quenching spectroscopy and synchronous fluorescence spectroscopy

Han, Ran; Liu, Baosheng; Li, Gaixia; Zhang, Qiuju

doi:10.1002/bio.2998

Cited by 15 publications

(2 citation statements)

References 34 publications

(35 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…However, the interaction of doxofylline with Lys altered the emission maxima peak with a redshift for Δλ = 15 nm, showing an increase in polarity around tyrosine and thereby lowering the hydrophobicity of it [27]. It is obvious from the data that interaction of doxofylline with Lys produced apparent changes in conformation of Lys [28]. Using the modified Stern-Volmer plot, K b was obtained as 2.29 × 10 4 M −1 .…”

Section: Synchronous Fluorescence Examinationmentioning

confidence: 98%

Studying the Mechanism of Interaction of Doxofylline with Human Lysozyme: A Biophysical and In Silico Approach

Alomar

2023

Molecules

View full text Add to dashboard Cite

In this study, multiple spectroscopic and computational methods were utilized to investigate the binding mechanism of doxofylline with lysozyme. The in vitro methods were used to obtain the binding kinetics and thermodynamics. UV–vis spectroscopy indicated the formation of complex between doxofylline and lysozyme. The Gibb’s free energy and binding constant from UV–vis data was obtained as −7.20 kcal M−1 and 1.929 × 105 M−1, respectively. Doxofylline successfully quenched the fluorescence of lysozyme, confirming the formation of complex. The kq and Ksv values for the quenching of lysozyme’s fluorescence by doxofylline were 5.74 × 1011 M−1 s−1 and 3.32 × 103 M−1, respectively. These values signified a moderate binding affinity between doxofylline and lysozyme. In synchronous spectroscopy, red shifts were observed for indicating the changes in microenvironment of lysozyme following the binding of doxofylline. The secondary structural analysis was determined using circular dichroism (CD) which revealed an increase in % α-helical as a result of doxofylline interaction. The binding affinity and flexibility of lysozyme upon complexation have been revealed via molecular docking and molecular dynamic (MD) simulations, respectively. According to the many parameters of the MD simulation, the lysozyme–doxofylline complex was stable under physiological conditions. All during the simulation time, hydrogen bonds were continuously present. The MM-PBSA binding energy for lysozyme and doxofylline binding was found to be −30.55 kcal mol−1.

show abstract

Section: Synchronous Fluorescence Examinationmentioning

confidence: 98%

Studying the Mechanism of Interaction of Doxofylline with Human Lysozyme: A Biophysical and In Silico Approach

Alomar

2023

Molecules

View full text Add to dashboard Cite

show abstract

“…It is classified into positive cooperativity, negative cooperativity and non-cooperativity according to the promotion or inhibition of the affinity for other ligand molecules. Usually, Hill's coefficient was used to determine the cooperativity of the drug and protein [35] , which can be calculated graphically on the basis of the following equation: Table 5. The values of n H were < 1 in the systems at different temperatures, which indicated that there is negative cooperation in the interaction of Cefpirome with Trypsin.…”

Section: Hill's Coefficient Of the Trypsin-cefpirome Systemmentioning

confidence: 99%

Spectroscopic and molecular modcking analysis of the interaction between Trypsin and Cefpirome

Liu¹,

Wang²,

Bian³

et al. 2017

JABST

Self Cite

View full text Add to dashboard Cite

The interaction between Cefpirome and Trypsin was studied using multi-spectroscopy and molecular docking methods. The results showed that quenching mechanism of the Trypsin-Cefpirome system was probably static. The main interaction force was electrostatic force, and the number of binding sites in this system was approximately equal to 1. The quenching curves indicated that the tyrosine and tryptophan residues were both involved in the reaction. Synchronous fluorescence spectroscopy further confirmed that the main binding site was closer to tryptophan residues. The distance (r) between Trypsin and Cefpirome was less than 7 nm, which indicated that the energy transfer from Trypsin to Cefpirome was non-radiative energy transfer. The values of the Hill's coefficients showed that there was negative cooperativity in the interaction between Cefpirome and Trypsin.

show abstract

Green Synthesis, in vitro Cytotoxicity, Antioxidant Activity and Interaction Studies of CuO Nanoparticles with DNA, Serum Albumin, Hemoglobin and Lysozyme

2022

View full text Add to dashboard Cite

The present study reports an environmentally safe synthesis of CuO NPs employing Echinophora platyloba DC extract. The production of CuO NPs was authenticated using various analytical characterization techniques such as FT-IR, TEM, XRD, SEM-EDX, DLS, zeta potential, and UV-Vis. The DPPH assay was employed to assess the scavenging efficacy of synthesized CuO NPs. The results of the MTT assay exhibited that CuO NPs have efficient anticancer potential on two used cancer cell lines (MCF-7 and Burkitt's lymphoma). Thus, it tempts us to study the synthesized CuO NPs biocompatible aspects by interactions with several biologically significant molecules. The present experimental evidence demonstrates the direct interaction of CuO NPs with DNA, which might be one of the credible highways elevating its anticancer potential. Moreover, we investigated the interaction of CuO NPs with the most important blood proteins (HSA, HHb, and Lys) in simulated physiological conditions using spectroscopic methods. The interaction findings suggest that the native conformation of the above proteins was preserved at the level of secondary structure in spite of complex formations with CuO NPs. The binding constant values revealed the greater binding affinity of CuO NPs with HSA, HHb, and Lys as compared to ct-DNA; the binding affinity was found in the order HSA > HHb > Lys > ct-DNA.

show abstract

Investigation on the interaction of cefpirome sulfate with lysozyme by fluorescence quenching spectroscopy and synchronous fluorescence spectroscopy

Cited by 15 publications

References 34 publications

Studying the Mechanism of Interaction of Doxofylline with Human Lysozyme: A Biophysical and In Silico Approach

Studying the Mechanism of Interaction of Doxofylline with Human Lysozyme: A Biophysical and In Silico Approach

Spectroscopic and molecular modcking analysis of the interaction between Trypsin and Cefpirome

Green Synthesis, in vitro Cytotoxicity, Antioxidant Activity and Interaction Studies of CuO Nanoparticles with DNA, Serum Albumin, Hemoglobin and Lysozyme

Contact Info

Product

Resources

About