Organophosphate flame retardants (OPFRs) pose the significant risks to the environment and human health and have become a serious public health issue. Tricresyl phosphates (TCPs), a group of aryl OPFRs, exhibit neurotoxicity and endocrine disrupting toxicity. However, the binding mechanisms between TCPs and human serum albumin (HSA) remain unknown. In this study, through fluorescence and ultraviolet-visible (UV-vis) absorption spectroscopy, molecular docking and molecular dynamics (MD), tri-para-cresyl phosphate (TpCP) was selected to explore potential interactions between HSA and TCPs. The results of the fluorescence spectroscopy demonstrated that a decrease in the fluorescence intensity of HSA and a blue shift were observed with the increasing concentrations of TpCP. The binding constant (Ka) was 2.575 × 104 L/mol, 4.701 × 104 L/mol, 5.684 × 104 L/mol and 9.482 × 104 L/mol at 293 K, 298 K, 303 K, and 310 K, respectively. The fluorescence process between HSA and TpCP involved a mix of static and dynamic quenching mechanism. The gibbs free energy (ΔG0) of HSA-TpCP system was -24.452 kJ/mol, -25.907 kJ/mol, -27.363 kJ/mol, and - 29.401 kJ/mol at 293 K, 298 K, 303 K, and 310 K, respectively, suggesting that the HSA-TpCP reaction was spontaneous. The enthalpy change (ΔH0) and thermodynamic entropy change (ΔS0) of the HSA-TpCP system were 60.83 kJ/mol and 291.08 J/(mol·>k), respectively, indicating that hydrophobic force was the major driving force in the HSA-TpCP complex. Furthermore, multispectral analysis also revealed that TpCP could alter the microenvironment of tryptophan residue and the secondary structure of HSA and bind with the active site I of HSA. Molecular docking and MD simulations confirmed that TpCP could spontaneously form a stable complex with HSA, which was consistent with the fluorescence experimental results. This study provides novel insights into the mechanisms of underlying the transportation and distribution of OPFRs in humans.

The development of natural inhibitors of polyphenol oxidase (PPO) is crucial in the prevention of enzymatic browning in fresh foods. However, few studies have focused on the effect of subsequent sterilization on their inhibition efficiency. This study investigated the influence and mechanism of high hydrostatic pressure (HHP) on the inhibition of PPO by epigallocatechin gallate (EGCG), cyanidin-3-O-glucoside (C3G), and ferulic acid. Results showed that under the conditions of 550 MPa/30 min, the activity of EGCG-PPO decreased to 55.92%, C3G-PPO decreased to 81.80%, whereas the activity of FA-PPO remained stable. Spectroscopic experiments displayed that HHP intensified the secondary structure transformation and fluorescence quenching of PPO. Molecular dynamics simulations revealed that at 550 MPa, the surface interaction between PPO with EGCG or C3G increased, potentially leading to a reduction in their activity. In contrast, FA-PPO demonstrated conformational stability. This study can provide a reference for the future industrial application of natural inhibitors.

Starch is the main source of energy and nutrition. Therefore, some merchants often illegally add cheaper starches to other types of starches or package cheaper starches as higher priced starches to raise the price. In this study, 159 samples of commercially available wheat starch, potato starch, corn starch and sweet potato starch were selected for the identification and classification based on multispectral techniques, including near-infrared (NIR), mid-infrared (MIR) and Raman spectroscopy combined with chemometrics, including pretreatment methods, characteristic wavelength selection methods and classification algorithms. The results indicate that all three spectral techniques can be used to discriminate starch types. The Raman spectroscopy demonstrated superior performance compared to that of NIR and MIR spectroscopy. The accuracy of the models after characteristic wavelength selection is generally superior to that of the full spectrum, and two-dimensional correlation spectroscopy (2D-COS) achieves better model performance than other wavelength selection methods. Among the four classification methods, convolutional neural network (CNN) exhibited the best prediction performance, achieving accuracies of 99.74 %, 97.57 % and 98.65 % in NIR, MIR and Raman spectra, respectively, without pretreatment or characteristic wavelength selection.

Plastic fragments are widely distributed in different environmental media and has recently drawn special attention due to its difficulty in degradation and serious health and environmental problems. Among, nanoplastics (NPs) are smaller in size, larger in surface/volume ratio, and more likely to easily adsorb ambient pollutants than macro plastic particles. Moreover, NPs can be easily absorbed by wide variety of organisms and accumulate in multiple tissues/organs and cells, thus posing a more serious threat to living organisms. Alpha-amylase (α-amylase) is a hydrolase, which can be derived from various sources such as animals, plants, and microorganisms. Currently, no studies have concentrated on the binding of NPs with α-amylase and their interaction mechanisms by employing a multidimensional strategy. Hence, we explored the interaction mechanisms of polystyrene nanoplastics (PS-NPs) with α-amylase by means of multispectral analysis, in vitro enzymatic activity analysis, and molecular simulation techniques under in vitro conditions. The findings showed that PS-NPs had the capability to bind with the intrinsic fluorescence chromophores, leading to fluorescence changes of these specific amino acids. This interaction also caused the alterations in the micro-environment of the fluorophore residues mainly tryptophan (TRP) and tyrosine (TYR) residues of α-amylase. PS-NPs interaction promoted the unfolding and partial expansion of polypeptide chains and the loosening of protein skeletons, and destroyed the secondary structure (increased random coil contents and decreased α-helical contents) of this protein, forming a larger particle size of the PS-NPs-α-amylase complex. Moreover, the enzymatic activity of α-amylase in vitro was found to be inhibited in a concentration dependent manner, thereby impairing its physiological functions. Further molecular simulation found that PS-NPs had a higher tendency to bind to the active site of α-amylase, which is the cause for its structural and functional changes. Additionally, the hydrophobic force played a major role in mediating the binding interactions between PS-NPs and α-amylase. Taken together, our study indicated that PS-NPs interaction can initiate the abnormal physiological functions of α-amylase through PS-NPs-induced structural and conformational alternations.

The drug-serum albumin interaction plays a dominant role in drug efficacy and disposition. The glycation of serum albumin that occurs during diabetes may affect its drug-binding properties in vivo. In order to evaluate the interactivity characteristics of cyanidin-3-O-glucoside (C3G) with human serum albumin (HSA) and glycated human serum albumin (gHSA), this study was undertaken using multiple spectroscopic techniques and molecular modeling analysis. Time-resolved fluorescence and the thermodynamic parameters indicated that the quenching mechanism was static quenching, and hydrogen bonding and Van der Waals force were the main forces. The protein fluorescence could be quenched by C3G, whereas the polarity of the fluorophore was not obviously changed. C3G significantly altered the secondary structure of the proteins. Furthermore, the interaction force that existed in the HSA-C3G system was greater than that in the gHSA-C3G system. Fluorescence excitation emission matrix spectra, red edge excitation shift, Fourier transform infrared spectroscopy and circular dichroism spectra provided further evidence that glycation could inhibit the binding between C3G and proteins. In addition, molecular modeling analysis supported the experimental results. The results provided more details for the application of C3G in the treatment of diabetes.