Effect of the presence of berberine/curcumin on the binding of limonin to human serum albumin and antitumor activity in vitro.

The competition among drugs for binding to plasma proteins is regarded as a pharmacokinetic drug interaction. Competition between antitumor agents and other drugs for plasma protein binding can alter the free concentration of the drug, potentially impacting its efficacy and increasing the risk of toxic side effects. Through a range of spectroscopic techniques, this study examined the interaction between limonin and human serum albumin (HSA) in the context of berberine (Ber) and curcumin (Cur) under physiological conditions to clarify the binding mechanisms of binary and ternary systems at the molecular level. As demonstrated by fluorescence quenching experiments, Static quenching was identified as the mechanism of interaction between HSA and limonin. The results of site competition experiments indicated that the binding site between limonin and HSA was site I, a result further supported by molecular docking simulations. Through the use of thermodynamic data calculations, it was determined that limonin forms a stable complex with HSA by establishing hydrogen bonds and van der Waals forces. Circular dichroism (CD) spectroscopy, three-dimensional (3D) fluorescence spectroscopy, and synchronous fluorescence spectroscopy (SFS) employed to validate the notion that limonin perturbed the microenvironment of amino acids and induced conformational changes in HSA. What's more, the presence of Ber or Cur was found to have further modified the alterations observed in the interaction between the original HSA-limonin binary system. In vitro cellular experiments showed that interaction with HSA reduced the antitumor activity of limonin. In contrast, adding Ber or Cur increased the inhibition rate of tumor cells. The coexistence of both Ber and Cur significantly diminished limonin's binding affinity to HSA. The current investigation enhances comprehension regarding the binding characteristics and interaction mechanisms involving limonin, Ber, Cur, and HSA. It explores the potential of HSA as a versatile drug carrier and furnishes theoretical underpinnings for co-administrative strategies.

Preparation of Ag3PO4/CoWO4 S-scheme heterojunction and study on sonocatalytic degradation of tetracycline.

In this study, 0.6Ag3PO4/CoWO4 composites were synthesized by hydrothermal method. The prepared materials were systematically characterized by techniques of scanning electron microscope (SEM), transmission electron microscope (TEM), X-ray diffractometer (XRD), X-ray photoelectron spectroscopy (XPS), N2 adsorption/desorption, and UV-vis diffuse reflectance spectrum (DRS). Furthermore, the sonocatalytic degradation performance of 0.6Ag3PO4/CoWO4 composites towards tetracycline (TC) was investigated under ultrasonic radiation. The results showed that, combined with potassium persulfate (K2S2O8), the 0.6Ag3PO4/CoWO4 composites achieved a high sonocatalytic degradation efficiency of 97.89 % within 10 min, which was much better than bare Ag3PO4 or CoWO4. By measuring the electrochemical properties, it was proposed that the degradation mechanism of 0.6Ag3PO4/CoWO4 is the formation of S-scheme heterojunction, which increases the separation efficiency of electron-hole pairs (e--h+) and generates more electrons and holes, thereby enhancing the degradation activity. The scavenger experiments confirmed that hole (h+) was the primary active substance in degrading TC, and free radicals (OH) and superoxide anion radical (O2-) were auxiliary active substances. The results indicated that 0.6Ag3PO4/CoWO4 nanocomposites could be used as an efficient and reliable sonocatalyst for wastewater treatment.