The impact of government subsidy programs on equity in health financing.

BACKGROUND: Iran government implemented the targeted subsidy plan in December 2010 to reduce energy consumption and inequality. In addition, the Health Transformation Plan was implemented by the Ministry of Health to reduce out-of-pocket payments. This study aimed to examine the impact of these two government subsidy programs on equity in health financing. METHOD: In this study, data on 528,046 households were collected using household surveys during 14 years (2007-2020). The Fairness in Financial Contribution index and Catastrophic Health Expenditures index were calculated. Also, a Logistic regression model was performed by the applied software of Stata V.14 to examine the effects of the two mentioned policies and other socioeconomic characteristics of households on their exposure to Catastrophic Health Expenditures. RESULTS: The FFC index was 0.829 and 0.795 respectively in 2007 and 2020. The trend analysis did not show significant changes in the FFC index between 2007 and 2020. TSP and HTP implementations do not reduce households' exposure to CHE significantly. Crowded households with more elder people, belonging to low-income deciles, without houses, and living in rural areas and deprived provinces, are more likely to be at risk of CHE. Health insurance coverage did not protect households from CHE. Highly educated and employed households were exposed to less CHE. CONCLUSION: The government subsidy programs have not been effective in improving FFC and reducing CHE indices. None of them has been able to realize the goal of the 6th National Development Plan of reducing CHE to 1%. The government should devise support packages for target households (households with more elderly people, lower incomes, without private houses, crowded, rural, and inhabited in deprived provinces), so they can protect households against CHE. Modifying and improving the quality of insurance coverage is strongly recommended due to its inefficiency.

A computational study on the interactions between a layered imine-based COF structure and selected anticancer drugs.

The covalent organic frameworks (COFs) are important materials in drug delivery. Herein, the interactions between an imine-based COF with selected commercially available anticancer drugs are studied. Molecular dynamics (MD) simulation studies were used. The studies were carried out in four different temperatures to find out the impact of the temperature on the binding free energies between the drugs and COF structure. It was found that the effect of temperature on binding free energy is ignorable. Between the hydrogen bonding, electrostatic, and van der Waals interactions, the last one is the most important one to keep the drug and COF next to each other. Also, the van der Waals interaction is keeping the layers of COF next to each other to create cavities. The cavities can be loaded with different drugs and the system can be used in drug delivery systems. Based on the obtained results, the drugs that are more lipophilic prefer to adhere more strongly to the COF in comparison with hydrophilic drugs.

A Computational Study on the Blocking Ability of Selected Commercially Available Anticancer Drugs and Their Hypothetic Derivatives on the CCR5.

Computational studies were done on the complexes between some commercially available anticancer drugs and their hypothetic derivatives and the CCR5 protein. At first step, the docking studies were done to obtain the best ligand that can inhibit the CCR5 protein. Based on the binding energy results obtained from the docking studies, 16 complexes were selected. Molecular dynamic studies were carried out on these structures and then molecular mechanics-generalized Born surface area calculations were done to find the binding energies of the ligands to the CCR5 protein. Based on the investigation of the binding modes of the ligands to the CCR5 protein, the TYR and ALA have more tendency to bind to the ligand moieties. By decomposing of the binding energies, it was found that the van der Waals interactions have the most important role in the binding of ligands to the protein in comparison with the electrostatic and hydrogen bonding interactions. The results of the interaction potential surface map analysis showed that the nitrogen and oxygen atoms have a relatively similar role in the binding of ligands to the CCR5 protein structure.