Biophysical study on the interaction between two palladium(II) complexes and human serum albumin by Multispectroscopic methods

Saeidifar, Maryam; Mansouri‐Torshizi, Hassan; Saboury, Ali Akbar

doi:10.1016/j.jlumin.2015.07.016

Cited by 61 publications

(18 citation statements)

References 60 publications

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“…Peak 1 ( λ ex = 280 nm and λ em = 335 nm) is related to the spectral characteristic of Tyr and Trp residues involving π → π* transition and reflects the polarity of the HSA microenvironment4243. Peak 2 ( λ ex = 225 nm and λ em = 328 nm) mainly exhibits the spectral behavior of the polypeptide chain backbone structure, and its fluorescence intensity is correlated with the secondary structure of the protein3438. Table 2 and Fig.…”

Section: Resultsmentioning

confidence: 99%

“…The possible shift in the position of the maximum emission wavelength of the amino acid residues corresponds to the changes in polarity in the vicinity of the chromophore molecule, revealing the conformational change in HSA3738. Miller39 proposed the long-standing theory that when Δλ was stabilized at 15 and 60 nm, the spectral characteristic information of tyrosine (Tyr) and tryptophan (Trp) residues of the protein were respectively observed.…”

Section: Resultsmentioning

confidence: 99%

“…Miller39 proposed the long-standing theory that when Δλ was stabilized at 15 and 60 nm, the spectral characteristic information of tyrosine (Tyr) and tryptophan (Trp) residues of the protein were respectively observed. A blue shift of λ max means that the amino acid residues are located in a hydrophobic environment, whereas a red shift of λ max implies that the amino acid residues are in a polar environment3840.…”

Section: Resultsmentioning

confidence: 99%

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Domain-specific interactions between MLN8237 and human serum albumin estimated by STD and WaterLOGSY NMR, ITC, spectroscopic, and docking techniques

Yang

Liu

Huang

et al. 2017

Sci Rep

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Alisertib (MLN8237) is an orally administered inhibitor of Aurora A kinase. This small-molecule inhibitor is under clinical or pre-clinical phase for the treatment of advanced malignancies. The present study provides a detailed characterization of the interaction of MLN8237 with a drug transport protein called human serum albumin (HSA). STD and WaterLOGSY nuclear magnetic resonance (NMR)-binding studies were conducted first to confirm the binding of MLN8237 to HSA. In the ligand orientation assay, the binding sites of MLN8237 were validated through two site-specific spy molecules (warfarin sodium and ibuprofen, which are two known site-selective probes) by using STD and WaterLOGSY NMR competition techniques. These competition experiments demonstrate that both spy molecules do not compete with MLN8237 for the specific binding site. The AutoDock-based blind docking study recognizes the hydrophobic subdomain IB of the protein as the probable binding site for MLN8237. Thermodynamic investigations by isothermal titration calorimetry (ITC) reveal that the non-covalent interaction between MLN8237 and HSA (binding constant was approximately 105 M−1) is driven mainly by favorable entropy and unfavorable enthalpy. In addition, synchronous fluorescence, circular dichroism (CD), and 3D fluorescence spectroscopy suggest that MLN8237 may induce conformational changes in HSA.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Domain-specific interactions between MLN8237 and human serum albumin estimated by STD and WaterLOGSY NMR, ITC, spectroscopic, and docking techniques

Yang

Liu

Huang

et al. 2017

Sci Rep

View full text Add to dashboard Cite

show abstract

“…These include molecular rearrangement, excited-state reactions, energy transfer, dynamic quenching (collisional quenching) and static quenching (ground-state complex formation) 14,28,29 . Any process that reduces the fluorescence intensity of a sample is called quenching of fluorescence.…”

Section: Fluorescence Spectroscopymentioning

confidence: 99%

The effect of spermine on the structure, thermal stability and activity of bovine pancreatic trypsin

et al. 2016

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This work studied the interaction between spermine and trypsin at pH 8.0. The thermal stability of trypsin was investigated in the presence of spermine over a temperature range (from 293 K to 353 K).Additionally, the conformational change of trypsin induced by spermine was analyzed by UV-Vis absorption and fluorescence spectra. The effect of spermine on trypsin activity was studied at 37 °C and pH 8.0, using Tris-HCl as a buffer. The fluorescence spectroscopy results indicated that the binding of spermine to trypsin was a spontaneous binding process. The fluorescence of trypsin was quenched by spermine through the static quenching mechanism. By increasing the concentration of spermine, the thermal stability of trypsin was increased. The quantitative analysis of CD spectra revealed some information regarding the changes in the content of the α-helix and the β-sheet of the trypsin upon binding to spermine. It was also found that by increasing the concentration of spermine, the activity of 2 trypsin was increased. Molecular docking results also revealed the presence of one binding site with a negative value for the Gibbs free energy of the binding of spermine to trypsin. Further, the docking and fluorescence spectroscopy study revealed that van der Waals interactions and hydrogen bonds played a major role in stabilizing the complex. As a result, spermine could be considered as an activator and stabilizer for trypsin.

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“…These compounds are of considerable interest because of a variety of their biological activities, e.g., anticancer [1], antitubercular [2], antibacterial [3], antifungal [4], anti-HIV [5], analgesic [6] and Human serum albumin (HSA), which is the main protein in human blood plasma, plays a pivotal role in the pharmacodynamic and pharmacokinetic properties because it can not only serve as a carrier for drugs, but also can participate in drug absorption, distribution and metabolism [10][11][12][13][14][15]. Interaction studies of HSA with biological molecules can elucidate the properties of the drug-protein complex because they may provide useful information about the structural features that determine the therapeutic effectiveness of drugs.…”

Section: Introductionmentioning

confidence: 99%

Comparative Interactions of Dihydroquinazolin Derivatives with Human Serum Albumin Observed via Multiple Spectroscopy

et al. 2017

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Abstract:The interactions of dihydroquinazolines with human serum albumin (HSA) were studied in pH 7.4 aqueous solution via fluorescence, circular dichroism (CD) and Fourier transform infrared (FTIR) spectroscopic techniques. In this work, 6-chloro-1-(3,3-dimethyl-butanoyl)-2-(un)substitutedphenyl-2,3-dihydroquinazolin-4(1H)-one (PDQL) derivatives were designed and synthesized to study the impact of five similar substituents (methyl, methoxy, cyano, trifluoromethyl and isopropyl) on the interactions between PDQL and HSA using a comparative methodology. The results revealed that PDQL quenched the intrinsic fluorescence of HSA through a static quenching process. Displacement experiments with site-specific markers revealed that PDQL binds to HSA at site II (subdomain IIIA) and that there may be only one binding site for PDQL on HSA. The thermodynamic parameters indicated that hydrophobic interactions mainly drove the interactions between PDQL and HSA. The substitution using five similar groups in the benzene ring could increase the interactions between PDQL and HSA to some extent through the van der Waals force or hydrogen bond effects in the proper temperature range. Isopropyl substitution could particularly enhance the binding affinity, as observed via comparative studies.

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Biophysical study on the interaction between two palladium(II) complexes and human serum albumin by Multispectroscopic methods

Cited by 61 publications

References 60 publications

Domain-specific interactions between MLN8237 and human serum albumin estimated by STD and WaterLOGSY NMR, ITC, spectroscopic, and docking techniques

Domain-specific interactions between MLN8237 and human serum albumin estimated by STD and WaterLOGSY NMR, ITC, spectroscopic, and docking techniques

The effect of spermine on the structure, thermal stability and activity of bovine pancreatic trypsin

Comparative Interactions of Dihydroquinazolin Derivatives with Human Serum Albumin Observed via Multiple Spectroscopy

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