Study of the interaction between ofloxacin and human serum albumin by spectroscopic methods

Lang

et al. 2015

New J. Chem.

In this paper, a potential anti-hepatoma Pt 4+ drug cis,cis,trans-[Pt(NH 3 ) 2 Cl 2 (O 2 CCH 2 CH 2 COOH)-(OCONHC 16 H 33 )] was synthesized and selected to investigate its binding to human serum albumin (HSA) by spectroscopy and molecular docking methods. Fluorescence spectra show that the Trp residue, the intrinsic fluorophore in HSA, was induced to a less hydrophobic microenvironment with the addition of the Pt 4+ compound, which induces the denaturation of HSA. Moreover, the fluorescence quenching mechanism was determined to be static quenching. The binding constant (K A ) and the number of binding sites (n) were calculated based on the results of fluorescence measurements. Circular dichroism (CD), Fourier transform infrared spectroscopy (FTIR) and three dimensional fluorescence spectroscopy proved that the Pt 4+ compound could slightly change the secondary structure and induce unfolding of the polypeptides of protein. Thermodynamic parameters indicate that the Pt 4+ compound binds to HSA through electrostatic attraction with one binding site. The molecular docking study indicated that parecoxib is embedded into site I (subdomain IIA) of HSA.

Section: Conformational Changes Of Hsa Induced By the Pt 4+ Compoundmentioning

confidence: 99%

Binding of a potential anti-hepatoma drug cis,cis,trans-[Pt(NH₃)₂Cl₂(O₂CCH₂CH₂COOH)-(OCONHC₁₆H₃₃)] with serum albumin – thermodynamic and conformational investigations

Lang

et al. 2015

New J. Chem.

“…Furthermore, with the addition of breviscapine solution, there was a slight red shift (from 345 to 348 nm) at the maximum wavelength of HSA fluorescence emission. This suggests that the chromophore of protein was placed in a more hydrophobic environment after addition of breviscapine . Figure A displays the Stern–Volmer plots at 278, 293, and 308 K. It shows that within the investigated concentrations range, the Stern–Volmer plot exhibited a good linear relationship, and the fluorescence data at different temperatures were analyzed using the Stern–Volmer equation as follows:

F_{0} / F = 1 + K_{normalq} τ_{0} [italicQ] = 1 + {italicK}_{SV} [italicQ]

…”

Section: Resultsmentioning

confidence: 99%

Binding of Breviscapine Toward Serum Albumin Studied by Spectroscopic and Electrochemical Techniques

Chang

Chen

et al. 2016

J Biochem Mol Toxicol

Breviscapine, a cerebrovascular drugs extracted from the Chinese herb Erigeron breviscapinus, has been frequently used to clinically treat cerebrovascular diseases such as cerebral thrombosis, cerebral infarction, and cerebral circulation insufficiency. In order to understand its pharmacology or toxicity, the binding mechanism of breviscapine to a model protein, human serum albumin (HSA), was probed by fluorescence, circular dichroism, Fourier transform infrared spectroscopy (FTIR), and electrochemical impedance spectroscopy approaches. The binding affinities and number of the drug with HSA were about 1.73 × 10(4) M(-1) and 0.99 at 293 K, respectively. The conformation of the protein was slightly altered after interacting with breviscapine. The drug-protein complex was mainly stabilized by electrostatic forces.

“…In the case of the reverse effect, it is considered to be a static quenching. The well‐known Stern–Volmer equation could be utilized to analyze the florescence quenching mechanism.

\frac{true}{{italicF}_{0}} = 1 + K_{S V} ([], Q)

where F 0 and F are the fluorescence intensity of GSH‐capped CdTe QDs in the absence and presence of a quencher (SCG), respectively; [Q] is the concentration of quencher (SCG) and K SV shows that the quenching efficiency of the quencher was the Stern–Volmer quenching constant.…”

Section: Resultsmentioning

confidence: 99%

“…In the case of the reverse effect, it is considered to be a static quenching. The well-known Stern-Volmer equation (26) could be utilized to analyze the florescence quenching mechanism.…”

Section: Possible Quenching Mechanismmentioning

confidence: 99%

Sensitive detection of sodium cromoglycate with glutathione‐capped CdTe quantum dots as a novel fluorescence probe

Hao

et al. 2015

Luminescence

A sensitive and simple analytical strategy for the detection of sodium cromoglycate (SCG) has been established based on a readily detectable fluorescence quenching effect of SCG for glutathione-capped (GSH-capped) CdTe quantum dots (QDs). The fluorescence of GSH-capped CdTe QDs could be efficiently quenched by SCG through electron transfer from GSH-capped CdTe QDs to SCG. Under optimum conditions, the response was linearly proportional to the concentration of SCG between 0.6419 and 100 µg/mL, with a correlation coefficient (R) of 0.9964; the detection limit (3δ/K) was 0.1926 µg/mL. The optimum conditions and the influence of coexisting foreign substances on the reaction were also investigated. The very effective and simple method reported here has been successfully applied to the determination of SCG in synthetic and real samples. It is believed that the established approach could have good prospects for application in the fields of clinical diseases diagnosis and treatment.