Probing the interaction of iron complex containing N3S2 macrocyclic ligand with bovine serum albumin using spectroscopic techniques

El-Shamy, Hany; Shaban, Shaban Y.; El‐Mehasseb, Ibrahim M.; El‐Kemary, Maged; Eldik, Rudi van

doi:10.1016/j.saa.2019.117811

Cited by 9 publications

(2 citation statements)

References 40 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…After interacting with Cu(II), like tryptones, all of the environmental protein-like substances exhibited an absorption significantly smaller than that of BSA [ p < 0.004 (Figure d)]. Therefore, the different spectroscopic behaviors of BSA and the other protein-like substances in their interaction with metal ions indicate their different complexation mechanisms. − …”

Section: Resultsmentioning

confidence: 99%

Why Should Tryptones Rather Than Bovine Serum Albumin Be Used as Model Proteins to Explore the Interactions between Proteins and Pollutants in Environments?

Gong

Qian

et al. 2021

Environ. Sci. Technol. Lett.

View full text Add to dashboard Cite

Because protein is readily degraded in the environment, it is unknown whether "protein-like substances" in environments are a group of intact proteins or a mixture of peptides and even amino acids. In this work, the widely adopted model protein bovine serum albumin (BSA) was compared with tryptones, an assortment of peptides, to evaluate their similarity with the proteins extracted from environmental samples. First, the physicochemical properties of BSA, tryptones, and the protein-like substances from the environmental samples were characterized, and the environmental protein-like substances and tryptones were found to have more aromatic groups than BSA and to be more unstable than BSA. Then, the interaction between proteins and metal ions or humic acids (HA) was examined. Differing from all of the other proteins, only the mixtures with BSA exhibited more significant fluorescence quenching and more positive specific ultraviolet−visible absorbance after interactions. Also, after binding to metal ions or HA, BSA tended to aggregate, while tryptones and the environmental protein-like substances did not. These results reveal that the environmental protein-like substances are more similar to tryptones than the model protein, BSA. Our work implies that tryptones, rather than BSA, should be a more appropriate alternative model in the investigation of protein−pollutant interactions.

show abstract

Section: Resultsmentioning

confidence: 99%

Why Should Tryptones Rather Than Bovine Serum Albumin Be Used as Model Proteins to Explore the Interactions between Proteins and Pollutants in Environments?

Gong

Qian

et al. 2021

Environ. Sci. Technol. Lett.

View full text Add to dashboard Cite

show abstract

“…As part of our focus on bioactive materials research [ 18 , 19 , 20 , 21 , 22 ], we report here on the binding of BSA to DBZ and DBZH 4 complexes using various techniques, e.g., UV–vis absorption and fluorescence, time-correlated single-photon counting, and cyclic voltammetry. The association constants, binding sites, and forces between the two complexes and BSA are reported, discussed, and correlated with the structure.…”

Section: Introductionmentioning

confidence: 99%

BSA Interaction, Molecular Docking, and Antibacterial Activity of Zinc(II) Complexes Containing the Sterically Demanding Biomimetic N3S2 Ligand: The Effect of Structure Flexibility

et al. 2022

Self Cite

View full text Add to dashboard Cite

Two zinc(II) complexes, DBZ and DBZH4, that have (ZnN3S2) cores and differ in the bridging mode of the ligating backbone, effectively bind to BSA. The binding affinity varies as DBZ > DBZH4 and depends on the ligand structure. At low concentrations, both complexes exhibit dynamic quenching, whereas at higher concentrations they exhibit mixed (static and dynamic) quenching. The energy transfer mechanism from the BSA singlet excited state to DBZ and DBZH4, is highly likely according to steady-state fluorescence and time-correlated singlet photon counting. Molecular docking was used to support the mode of interaction of the complexes with BSA and showed that DBZ had more energy for binding. Furthermore, antibacterial testing revealed that both complexes were active but to a lesser extent than chloramphenicol. In comparison to DBZH4, DBZ has higher antibacterial activity, which is consistent with the binding constants, molecular docking, and particle size of adducts. These findings may have an impact on biomedicine.

show abstract

Recent advances in iron complexes and their interaction with nucleic acids

Parveen

2023

Nucleic Acids

View full text Add to dashboard Cite

Probing the interaction of iron complex containing N3S2 macrocyclic ligand with bovine serum albumin using spectroscopic techniques

Cited by 9 publications

References 40 publications

Why Should Tryptones Rather Than Bovine Serum Albumin Be Used as Model Proteins to Explore the Interactions between Proteins and Pollutants in Environments?

Why Should Tryptones Rather Than Bovine Serum Albumin Be Used as Model Proteins to Explore the Interactions between Proteins and Pollutants in Environments?

BSA Interaction, Molecular Docking, and Antibacterial Activity of Zinc(II) Complexes Containing the Sterically Demanding Biomimetic N3S2 Ligand: The Effect of Structure Flexibility

Recent advances in iron complexes and their interaction with nucleic acids

Contact Info

Product

Resources

About