Spectroscopic analyses on interaction of Naphazoline hydrochloride with bovine serum albumin

Zhu, Shunzhi; Liu, Yang

doi:10.1016/j.saa.2012.08.040

Cited by 42 publications

(8 citation statements)

References 44 publications

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“…From the linear fit of log [(F 0 −F)/F] versus the concentration of apocynin to the equation, a K a value of 2.19 × 10 4 M −1 was obtained and “n”, the number of binding sites, was calculated as 1.002; an indication that there is only one association between apocynin and HSA (Figure 8c). It is important to note that the obtained value of the apparent binding constant has the same magnitude compared to several molecules which are able to bind to has; for instance, ascorbic acid K a = 2.24 × 10 4 M −1 [34], salvinolic acid K a = 7.36 × 10 4 M −1 [35] and naphazoline K a = 2.60 ×10 3 M −1 [36]. Hence, we can assume that apocynin can be transported by albumin.…”

Section: Resultsmentioning

confidence: 98%

Apocynin: Chemical and Biophysical Properties of a NADPH Oxidase Inhibitor

et al. 2013

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Apocynin is the most employed inhibitor of NADPH oxidase (NOX), a multienzymatic complex capable of catalyzing the one-electron reduction of molecular oxygen to the superoxide anion. Despite controversies about its selectivity, apocynin has been used as one of the most promising drugs in experimental models of inflammatory and neurodegenerative diseases. Here, we aimed to study the chemical and biophysical properties of apocynin. The oxidation potential was determined by cyclic voltammetry (Epa = 0.76V), the hydrophobicity index was calculated (logP = 0.83) and the molar absorption coefficient was determined ( 275nm = 1.1 × 10). Apocynin was a weak free radical scavenger (as measured using the DPPH, peroxyl radical and nitric oxide assays) when compared to protocatechuic acid, used here as a reference antioxidant. On the other hand, apocynin was more effective than protocatechuic acid as scavenger of the non-radical species hypochlorous acid. Apocynin reacted promptly with the non-radical reactive species H 2 O 2 only in the presence of peroxidase. This finding is relevant, since it represents a new pathway for depleting H 2 O 2 in cellular experimental models, besides the direct inhibition of NADPH oxidase. This could be relevant for its application as an inhibitor of NOX4, since this isoform produces H 2 O 2 and not superoxide anion. The binding parameters calculated by fluorescence quenching showed that apocynin binds to human . The association did not alter the secondary and tertiary structure of HSA, as verified by synchronous fluorescence and circular dichroism. The displacement of fluorescent probes suggested that apocynin binds to site I and site II of HSA. Considering the current biomedical applications of this phytochemical, the dissemination of these chemical and biophysical properties can be very helpful for scientists and physicians interested in the use of apocynin.

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Section: Resultsmentioning

confidence: 98%

Apocynin: Chemical and Biophysical Properties of a NADPH Oxidase Inhibitor

et al. 2013

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“…Its spectra could provide much valuable information about the microenvironment around fluorophores in biomacromolecules. For protein molecules, when the Δ λ = 15 nm is fixed, the spectrum characteristic of tyrosine (Tyr) residues can be observed, and when Δ λ = 60 nm is fixed, the spectrum characteristic of Trp residues can be obtained in general [ 25 – 27 ]. In this study, the synchronous fluorescence spectroscopy was used to estimate the binding site of SAC to HSA molecules.…”

Section: Resultsmentioning

confidence: 99%

Study on the interaction of bioactive compound S-allyl cysteine from garlic with serum albumin

Sun

Wang

2017

Journal of Food and Drug Analysis

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Multispectroscopic techniques were used to investigate the interaction of S-allyl cysteine (SAC) from garlic with human serum albumin (HSA). UV-Vis absorption measurements prove the formation of the HSA-SAC complex. An analysis of fluorescence spectra revealed that in the presence of SAC, the quenching mechanism of HSA is considered static. The quenching rate constant K, K, and the binding constant K were estimated. According to the Van't Hoff equation, the thermodynamic parameters enthalpy change (ΔH) and entropy change (ΔS) were calculated to be -1.00×10 J/mol and -255 J/mol/K, respectively. These indicate that hydrogen bonds and van der Waals forces are the major forces between SAC and HSA. The changes in the secondary structure of HSA, which was induced by SAC, were determined by circular dichroism spectroscopy. Energy transfer was confirmed and the distance between donor and acceptor was calculated to be 2.83 nm.

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“…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.

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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.

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Spectroscopic analyses on interaction of Naphazoline hydrochloride with bovine serum albumin

Cited by 42 publications

References 44 publications

Apocynin: Chemical and Biophysical Properties of a NADPH Oxidase Inhibitor

Apocynin: Chemical and Biophysical Properties of a NADPH Oxidase Inhibitor

Study on the interaction of bioactive compound S-allyl cysteine from garlic with serum albumin

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

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