Mechanical properties of discarded shield residue improved by calcium carbide slag and fly ash as subgrade filling.

To utilize discarded shield residue and alleviate the shortage of subgrade filling, industrial wastes such as calcium carbide slag (CCS) and fly ash (FA) were considered to enhance the mechanical properties of the shield residue. A series of laboratory tests, including California Bearing Ratio (CBR) tests, unconfined compressive strength (UCS) tests, moisture content tests, pH tests, water stability tests, and dry-wet cycles tests were performed on discarded shield residue with additive contents. The results show that the UCS and CBR values enhanced significantly with the increase in curing time.

Spectroscopic and cytotoxicity studies on the combined interaction of (-)-epigallocatechin-3-gallate and anthracycline drugs with human serum albumin.

The interactions of (-)-epigallocatechin-3-Gallate (EGCG) and anthracycline drugs (doxorubicin, DOX and epirubicin, EPI) alone or in combination with human serum albumin (HSA) under physiological condition were studied by fluorescence spectroscopy, UV-vis absorption spectroscopy, circular dichroism (CD) spectroscopy, and dynamic light scattering (DLS). The cytotoxic activity of the single drug, combined drugs, and their complexes with HSA against human cervical cancer HeLa cell line was determined by MTT assay. Fluorescence quenching result and difference spectra of UV absorption revealed the formation of static complex between EGCG, DOX, or EPI and HSA.

Mutual influence of piceatannol and bisphenol F on their interaction with pepsin: Insights from spectroscopic, isothermal titration calorimetry and molecular modeling studies.

The individual and combined interactions of bisphenol F and piceatannol with pepsin were investigated using spectroscopic methods (fluorescence, UV-vis absorption, and circular dichroism spectroscopy), combined with isothermal titration calorimetry and molecular docking. Thermodynamic data showed that hydrogen bonds and van der Waals forces might play a major role for the binding process. Site marking experiments and molecular docking confirmed the binding sites of these two ligands on pepsin.