Spectroscopic investigation on the interaction of some polymer–cobalt(III) complexes with serum albumins

Vignesh, Gopalaswamy; Manojkumar, Yesaiyan; Sugumar, K.; Arunachalam, S.

doi:10.1016/j.jlumin.2014.08.045

Cited by 57 publications

(11 citation statements)

References 25 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…2(b), it can be seen that when compared with free state HSA, different concentrations of caffeic acid cannot cause any observable changes in HSA fluorescence lifetime. Thus dynamic collision is not the main reason for HSA quenching and static quenching of HSA by caffeic acid was confirmed (43).…”

Section: Resultsmentioning

confidence: 82%

Fluorescence spectroscopy and molecular simulation on the interaction of caffeic acid with human serum albumin

Xiang

Duan

et al. 2016

Luminescence

View full text Add to dashboard Cite

Fluorescence spectroscopy and molecular simulation were explored to study the interaction between caffeic acid and human serum albumin (HSA). The experimental results indicated that the fluorescence quenching mechanism between caffeic acid and HSA is a static quenching, which was proved again by the analysis of fluorescence lifetime by time-correlated single photon counting. The binding process is spontaneous and the hydrophobic force is the main force between caffeic acid and HSA. In addition, the binding of caffeic acid to HSA was modeled by molecular dynamics simulations. The root mean square deviations, root mean square fluctuations, radius of gyration and the number of hydrogen bonds of the molecular dynamic (MD) simulation process were analyzed. Both experimental and modeling results demonstrated strong binding between HSA and caffeic acid. HSA had a slight conformational change when it binds with caffeic acid. The obtained information is useful for HSA drug design. Copyright © 2016 John Wiley & Sons, Ltd.

show abstract

Section: Resultsmentioning

confidence: 82%

Fluorescence spectroscopy and molecular simulation on the interaction of caffeic acid with human serum albumin

Xiang

Duan

et al. 2016

Luminescence

View full text Add to dashboard Cite

show abstract

“…For the static quenching process, the binding constant (K b ) and the number of binding sites (n) can be determined by the following equation 62 where F 0 and F are the fluorescence intensities of the emitter in the absence and presence of the quencher, respectively, and [Q] the concentration of the quencher. Thus, a plot of log F 0 − F/F versus log [Q] (Fig.…”

Section: Resultsmentioning

confidence: 99%

Biomolecular Interaction, Anti-Cancer and Anti-Angiogenic Properties of Cobalt(III) Schiff Base Complexes

Ambika

Manojkumar

Arunachalam

et al. 2019

Sci Rep

View full text Add to dashboard Cite

Two cobalt(III) Schiff base complexes, trans-[Co(salen)(DA) 2 ](ClO 4 ) ( 1 ) and trans-[Co(salophen)(DA) 2 ](ClO 4 ) ( 2 ) (where salen: N,N’-bis(salicylidene)ethylenediamine, salopen: N,N’-bis(salicylidene)-1,2-phenylenediamine, DA: dodecylamine) were synthesised and characterised using various spectroscopic and analytical techniques. The binding affinity of both the complexes with CT-DNA was explored adopting UV-visible, fluorescence, circular dichroism spectroscopy and cyclic voltammetry techniques. The results revealed that both the complexes interacted with DNA via intercalation as well as notable groove binding. Protein (BSA) binding ability of these complexes was investigated by absorption and emission spectroscopy which indicate that these complexes engage in strong hydrophobic interaction with BSA. The mode of interaction between these complexes and CT-DNA/BSA was studied by molecular docking analysis. The in vitro cytotoxic property of the complexes was evaluated in A549 (human small cell lung carcinoma) and VERO (African green monkey kidney cells). The results revealed that the complexes affect viability of the cells. AO and EB staining and cell cycle analysis revealed that the mode of cell death is apoptosis. Both the complexes showed profound inhibition of angiogenesis as revealed in in-vivo chicken chorioallantoic membrane (CAM) assay. Of the two complexes, the complex 2 proved to be much more efficient in affecting the viability of lung cancer cells than complex 1 . These results indicate that the cobalt(III) Schiff base complexes in this study can be potentially used for cancer chemotherapy and as inhibitor of angiogenesis, in general, and lung cancer in particular, for which there is need for substantiation at the level of signalling mechanisms and gene expressions.

show abstract

“…The static quenching confirmed the quenching mechanism in this study (Figure 4). 17 3.4. Analysis of Binding and Its Thermodynamic Properties.…”

Section: Resultsmentioning

confidence: 99%

Comparative Studies on the Interaction of Spermidine with Bovine Trypsin by Multispectroscopic and Docking Methods

Momeni

Shareghi

Saboury³

et al. 2016

J. Phys. Chem. B

View full text Add to dashboard Cite

The effect of spermidine on the kinetics, conformation, and dynamics of native trypsin was studied by steady-state thermal stability, intrinsic fluorescence, circular dichroism (CD), ultraviolet-visible (UV-vis) spectroscopy, and kinetic techniques, as well as molecular docking, at the temperatures of 298 and 308 K. The Stern-Volmer quenching constants (Ksv) for the trypsin-spermidine complex were obtained at two temperatures, revealing that spermidine quenched the intensity of trypsin through the static mode of the quenching mechanism. The corresponding thermodynamic parameters, Gibbs free-energy, enthalpy, and entropy changes, showed that the binding process was spontaneous. These values and the molecular docking technique revealed that the hydrogen bonding and van der Waals forces played a major role in stabilizing the complex. CD, absorption, and fluorescence results also indicated that spermidine binding had a partial effect on trypsin structure. Spermidine could also influence the activity of trypsin. Upon spermidine binding, the Vmax value of the enzyme was increased and the kcat/Km values were enhanced slightly. The Tm of the trypsin-spermidine complex was enhanced probably due to the higher H-bond formation and lower surface hydrophobicity after spermidine modification, as confirmed by UV-vis spectroscopy and fluorescence spectra. UV absorption and CD studies also indicated that the binding of spermidine to trypsin had induced microenvironmental changes around the enzyme, leading to changes in its secondary structure.

show abstract

Spectroscopic investigation on the interaction of some polymer–cobalt(III) complexes with serum albumins

Cited by 57 publications

References 25 publications

Fluorescence spectroscopy and molecular simulation on the interaction of caffeic acid with human serum albumin

Fluorescence spectroscopy and molecular simulation on the interaction of caffeic acid with human serum albumin

Biomolecular Interaction, Anti-Cancer and Anti-Angiogenic Properties of Cobalt(III) Schiff Base Complexes

Comparative Studies on the Interaction of Spermidine with Bovine Trypsin by Multispectroscopic and Docking Methods

Contact Info

Product

Resources

About