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This study is to theoretically and experimentally investigate the propagation of stress waves in the filled joint set. The time-domain recursive method is used to derive the propagation equations in the filled joint set, and the filled joints are further simplified into structural planes without joint thickness. The split-Hopkinson rock bar is modified to simulate P wave propagation normally across the parallel filled joints. The relationship among stress-closure curve, joint specific stiffness, transmission coefficient and loading rate is analyzed. The results show that, for the rock mass with a single joint, both the joint specific stiffness and transmission coefficient of different filling materials increase with loading rate. More serious particle breakage of the filling materials leads to lower joint specific stiffness and transmission coefficient. For the rock mass with two joints, the joint specific stiffness of each joint affects the transmission coefficient of the filled joint set. It is found that our theoretical calculations are basically consistent with the experimental ones, and the joint specific stiffness can well characterize the propagation behavior of stress wave in the filled parallel rock joints. [ABSTRACT FROM AUTHOR]

To explore the effect of the joint contact area and temperature on the dynamic property of rock joints and wave propagation in granite rockmass, an impact test of a jointed granite specimen was conducted with a split–Hopkinson pressure bar. The jointed specimen was composed of an artificially grooved specimen and an intact specimen. The ratio of the joint contact area to the cross-sectional area of the intact specimen was defined as the joint matching coefficient (JMC). The specimens were heat-treated at temperatures of 25°C, 200°C, 400°C, and 600°C. The experimental results showed that with the decrease in the JMC, the nonlinear characteristic of the stress–strain curve for the initial loading segment was more evident for the heat-treated specimen at a constant temperature. Furthermore, the transmitted coefficient, secant modulus, and joint-specific stiffness gradually decreased. For a given JMC, the expansion of the mineral component in the specimen heat-treated at 200°C caused the internal cracks to close, resulting in a larger transmitted coefficient and joint-specific stiffness. For the specimens heat-treated at 400°C and 600°C, the transmitted coefficient and joint-specific stiffness gradually decreased owing to thermal damage. In addition, the deformation of the jointed specimen at different temperatures was mainly caused by joint closure. A smaller JMC or more serious thermal damage led to an increase in the peak value of the joint closure. [ABSTRACT FROM AUTHOR]

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Cisplatin and its analogues are widely used as chemotherapeutic agents in clinical practice. After being intravenously administrated, a substantial amount of platinum will bind with proteins in the blood. This binding is vital for the transport, distribution, and metabolism of drugs; however, toxicity can also occur from the irreversible binding between biologically active proteins and platinum drugs. Therefore, it is very important to study the protein-binding behavior of platinum drugs in blood. This review summarizes mass spectrometry-based strategies to identify and quantitate the proteins binding with platinum anticancer drugs in blood, such as offline high-performance liquid chromatography/inductively coupled plasma mass spectrometry (HPLC–ICP-MS) combined with electrospray ionization mass spectrometry (ESI-MS/MS) and multidimensional LC–ESI-MS/MS. The identification of in vivo targets in blood cannot be accomplished without first studying the protein-binding behavior of platinum drugs in vitro; therefore, relevant studies are also summarized. This knowledge will further our understanding of the pharmacokinetics and toxicity of platinum anticancer drugs, and it will be beneficial for the rational design of metal-based anticancer drugs. [ABSTRACT FROM AUTHOR]

The discovery of the anticancer activity of cisplatin and its clinical application has opened a new field for studying metal-coordinated anticancer drugs. Metal-based anticancer drugs, such as cisplatin, can be transported to cells after entering into the human body and form metal–DNA or metal–protein adducts. Then, responding proteins will recognize adducts and form stable complexes. The proteins that were binding with metal-based anticancer drugs were relevant to their mechanism of action. Herein, investigation of the recognition between metal-based anticancer drugs and its binding partners will further our understanding about the pharmacology of cytotoxic anticancer drugs and help optimize the structure of anticancer drugs. The "soft" ionization mass spectrometric methods have many advantages such as high sensitivity and low sample consumption, which are suitable for the analyses of complex biological samples. Thus, MS has become a powerful tool for the identification of proteins binding or responding to metal-based anticancer drugs. In this review, we focused on the mass spectrometry-based quantitative strategy for the identification of proteins specifically responding or binding to metal-based anticancer drugs, ultimately elucidating their mechanism of action. [ABSTRACT FROM AUTHOR]

Cisplatin is widely used for the treatment of various solid tumors. It is mainly administered by intravenous injection, and a substantial amount of the drug will bind to plasma proteins, a feature that is closely related to its pharmacokinetics, activity, toxicity, and side effects. However, due to the unique properties of platinum complexes and the complexity of the blood proteome, existing methods cannot systematically identify the binding proteome of cisplatin in blood. In this study, high-abundance protein separation and an ion mobility mass spectrometry-based 4D proteomic method were combined to systematically and comprehensively identify the binding proteins of cisplatin in blood. The characteristic isotope patterns of platinated peptides and a similarity algorithm were utilized to eliminate false-positive identification. Finally, 39 proteins were found to be platinated. Bioinformatics analysis showed that the identified proteins were mainly involved in the complement and coagulation cascade pathways. The binding ratio of some peptides with cisplatin was measured based on the area ratio of the free peptide using the parallel reaction monitoring method. This study provides a new method for systematically identifying binding proteins of metal drugs in blood, and the identified proteins might be helpful for understanding the toxicity of platinum anticancer drugs.