Pengfei Qin

New Insights into the Behavior of Bovine Serum Albumin Adsorbed onto Carbon Nanotubes: Comprehensive Spectroscopic Studies

Bovine serum albumin (BSA) nonspecifically binds to well-dispersed multiwalled carbon nanotubes (MWCNTs), forming a stable bioconjugate. After accounting for the inner filter effect, we found the fluorescence intensity of BSA was quenched by MWCNTs in static mode, which was authenticated by lifetime measurements and Stern-Volmer calculations. The thermodynamic parameters DeltaG(o), DeltaS(o), and DeltaH(o) were -9.67 x 10(3) + 2.48 x 10(3) ln lambda J x mol(-1), 41.0 - 0.828 ln lambda J x mol(-1) x K(-1), and 7.30 x 10(3) + 2.23 x 10(3) ln lambda J x mol(-1) (lambda < 1 x 10(-4)), respectively, which shows a spontaneous and electrostatic interaction. Scatchard analysis and UV-visible results provide statistical data concerning changes in the microenvironment of amide moieties in response to different doses of MWCNTs, revealing different behavior of the BSA molecules. The absorption spectra also show that the tertiary structure of the protein was partially destroyed. The content of secondary structure elements of BSA was changed by the tubes. This work elucidates the interaction mechanism of BSA and MWCNTs from a spectroscopic angle.

Characterizing the Interaction between Tartrazine and Two Serum Albumins by a Hybrid Spectroscopic Approach

Tartrazine is an artificial azo dye commonly used in food products. The present study evaluated the interaction of tartrazine with two serum albumins (SAs), human serum albumin (HSA) and bovine serum albumin (BSA), under physiological conditions by means of fluorescence, three-dimensional fluorescence, UV-vis absorption, and circular dichroism (CD) techniques. The fluorescence data showed that tartrazine could bind to the two SAs to form a complex. The binding process was a spontaneous molecular interaction procedure, in which van der Waals and hydrogen bond interactions played a major role. Additionally, as shown by the UV-vis absorption, three-dimensional fluorescence, and CD results, tartrazine could lead to conformational and some microenvironmental changes of both SAs, which may affect the physiological functions of SAs. The work provides important insight into the mechanism of toxicity of tartrazine in vivo.

Impact of carbon chain length on binding of perfluoroalkyl acids to bovine serum albumin determined by spectroscopic methods.

Perfluoroalkyl acids (PFAAs), an emerging class of globally environmental contaminants, pose a great threat to humans with wide exposure from food and other potential sources. To evaluate the toxicity of PFAAs at the protein level, the effects of three PFAAs on bovine serum albumin (BSA) were characterized by fluorescence spectroscopy, synchronous fluorescence spectroscopy, and circular dichroism (CD). On the basis of the fluorescence spectra and CD data, we concluded that perfluoropentanoic acid (PFPA) had little effect on BSA. However, perfluorooctanoic acid (PFOA) and perfluorodecanoic acid (PFDA) exhibited remarkable fluorescence quenching, which was attributed to the formation of a moderately strong complex. The enthalpy change (DeltaH) and entropy change (DeltaS) indicated that van der Waals forces and hydrogen bonds were the dominant intermolecular forces in the binding of PFAAs to BSA. Furthermore, the BSA conformation was slightly altered in the presence of PFOA and PFDA, with a reduction of alpha helix. These results indicated that PFAAs indeed impact the conformation of BSA, and PFAAs with longer carbon chains were more toxic, especially at lower concentrations.

Toxic effects of ethanol on bovine serum albumin

The toxic effects of ethanol on bovine serum albumin (BSA) were measured by resonance light scattering (RLS), fluorescence spectroscopy, ultraviolet spectrophotometry (UV), circular dichroism (CD), and transmission electron microscopy (TEM). The results indicated that ethanol had toxic effects on BSA, which led to protein denaturation and the effects increased with the ethanol dose. By means of RLS, BSA was found to aggregate in the presence of ethanol and particles smaller than 100 nm were observed from TEM. The fluorescence spectra showed that the intensity of the characteristic peak of BSA decreased and blue shifted, because of changes in the BSA skeleton structure, as well as alteration of the microenvironment of tryptophan (Trp) residues. The conformation changes of BSA were also shown by UV and CD spectrometry.

Oxidative stress response of two fluoroquinolones with catalase and erythrocytes: A combined molecular and cellular study

Ciprofloxacin (CPFX) and enrofloxacin (ENFX), two representatives of fluoroquinolones (FQs), pose potential threats to health for their wide exposures in environment. The aim of the study is to characterize the harmful effects of oxidative stress induced by CPFX and ENFX from the structure and function of catalase (CAT), a vital enzyme involved in protection against oxidative damage. The cellular tests firstly confirmed an enhanced oxidative stress in FQs treated erythrocytes from the depletion of GSH contents and decrease of CAT activity. Besides, CPFX posed more of an oxidative threat than ENFX. During the spectroscopic and computational investigations, both FQs could bind into its central cavity with only one binding site and interact with Arg 65, Arg 362 and His 363 mainly through electrostatic forces. Furthermore, the binding of two FQs not only caused the conformational and micro-environmental changes of CAT, but also inhibited its molecular activity, consistent with the cellular activity measurements. All these results suggested that the structural and functional changes of CAT were closely associated with increased risk of oxidative stress induced by both FQs. The established methods in this work can help to comprehensively understanding the oxidative stress-induced cellular damage of other pollutants via antioxidant effects.

A new strategy to probe the genotoxicity of silver nanoparticles combined with cetylpyridine bromide

The environmental genotoxic behavior of silver nanoparticles (nanoAg) combined with the detergent cetylpyridine bromide (CPB) was examined in vitro. The experimental results showed that the genotoxicity of nanoAg itself is weak, but nanoAg shows obvious genotoxicity after combined with CPB. The combined materials have a strong coeffect on calf thymus DNA (ctDNA) at a concentration of 3.3 x 10(-6 )gmL(-1) nanoAg and 6.0 x 10(-6) molL(-1) CPB. After the addition of ctDNA to the nanoAg-CPB system, the particles are scattered and the diameter decreases, which indirectly reveal that nanoAg-CPB has genotoxicity.

Perfluorodecanoic Acid Binding to Hemoproteins: New Insights from Spectroscopic Studies

Perfluorodecanoic acid (PFDA), a representative of the perfluoroalkyl acids, poses a great threat to humans and animals via food and other potential sources. In this work, we determined the effects of PFDA binding to two hemoproteins, bovine hemoglobin (BHb) and myoglobin (Mb). Using fluorescence spectroscopy, we found that PFDA greatly enhanced the fluorescence intensity of both hemoproteins, while perfluorooctanoic acid (PFOA) and perfluoropentanoic acid (PFPA) have minimal effects on the fluorescence. UV-vis absorption (UV) spectroscopy showed that PFDA induced the unfolding of the hemoproteins accompanied by exposure of the heme pocket and facilitating the formation of hemichrome. Additionally, as shown by the circular dichroism (CD) data, PFDA altered the secondary structure of both BHb and Mb. This work elucidates the interaction mechanism of PFDA with two hemoproteins.

Toxic interaction between acid yellow 23 and trypsin: spectroscopic methods coupled with molecular docking.

Acid yellow 23 (AY23) is a pervasive azo dye used in many fields which is potentially harmful to the environment and human health. This paper studied the toxic effects of AY23 on trypsin by spectroscopic and molecular docking methods. The addition of AY23 effectively quenched the intrinsic fluorescence of trypsin via static quenching with association constants of K290,K = 3.67 × 105 L mol−1 and K310,K = 1.83 × 105 L mol−1. The calculated thermodynamic parameters conformed that AY23 binds to trypsin predominantly via electrostatic forces with one binding site. Conformational investigations indicated the skeletal structure of trypsin unfolded and the microenvironment of tryptophan changed with the addition of AY23. Molecular docking study showed that AY23 interacted with the His 57 and Lys 224 residue of trypsin and led to the inhibition of enzyme activity. This study offers a more comprehensive picture of AY23–trypsin interaction and indicates their interaction may perform toxic effects within the organism.

Spectroscopic investigation on the toxic interaction of melamine with herring sperm DNA.

The toxic interaction of melamine with herring sperm DNA (hs‐DNA) was investigated by using fluorescence and UV–vis absorption spectra techniques. The experimental results showed that the toxic interaction between melamine and hs‐DNA occurred. Fluorescence quenching experiments indicated the existence of electrostatic binding between melamine and hs‐DNA. The binding constants KA and the binding site numbers were calculated by means of the Stern–Volmer equation and were 9.8 × 104 L mol−1 and 1.3, respectively. Both the results of fluorescence spectra and UV–vis absorption spectra verified that there are electrostatic binding between melamine and hs‐DNA. The possibility in the presence of a classical intercalation binding mode could be ruled out by using DNA unwinding experiments.

Assessing the potential toxic effect of one persistent organic pollutant: non-covalent interaction of dicofol with the enzyme trypsin.

Because of the widespread concern that persistent organic pollutants (POPs) may be adversely affecting the health of humans, reliable assessing their toxic effects is urgently needed. We selectively study the interaction between dicofol (DCF) and trypsin by steady state and time resolved fluorescence quenching measurements and UV-visible absorption spectroscopy under physiological conditions as well as applying molecular docking method to establish the interaction model. The fluorescence results indicate DCF can spontaneously form a complex with trypsin mainly by hydrogen bond with only one binding site, which had been validated in molecular docking. The conformational change of trypsin was proved by UV-visible absorption and synchronous fluorescence spectroscopy indicating a red shift of carbonyl absorption peak. All the results indicated DCF had potential toxic effects on both the structure and activity of the enzyme trypsin and the effects enhanced with the increasing concentration of DCF.