The economy of Saudi Arabia is currently undergoing a major transformation which will have an impact on employment in the pharmacy sector. However, quantitative data characterizing the pharmacy workforce in the Kingdom are currently not available. Therefore, the aim of this study was to determine the current status of the licensed pharmacy workforce in the pharmacy field in Saudi Arabia. Descriptive statistics were performed on data from the Saudi Commission for Health Specialties (SCFHS) as of March 2017. The labor market for pharmacists in Saudi Arabia is dominated by expatriates. Saudi nationals constitute less than 20% of the pharmacists employed in the Kingdom. The underemployment of Saudis is most evident in the largest sectors of the pharmacy field, namely, private health care establishments, community pharmacies, and pharmaceutical companies. There is an unmet need to train Saudi citizens as pharmacists and retain them in the workforce. Addressing this issue should become an important objective in Saudi Arabia’s Vision for 2030.

Rivaroxaban is a direct inhibitor of coagulation factor Xa and is used for venous thromboembolic disorders. The rivaroxaban interaction with BSA was studied to understand its PK and PD (pharmacokinetics and pharmacokinetics) properties. Multi-spectroscopic studies were used to study the interaction which included UV spectrophotometric, spectrofluorometric and three dimensional spectrofluorometric studies. Further elucidation of data was done by molecular simulation studies to evaluate the interaction behavior between BSA and rivaroxaban. Rivaroxaban quenched the basic fluorescence of BSA molecule by the process of static quenching since rivaroxaban and BSA form a complex that results in shift of the absorption spectra of BSA molecule. A decline in the values of binding constants was detected with the increase of temperatures (298–308 K) and the binding constants were in range from 1.32 × 105 to 4.3 × 103 L mol−1 indicating the instability of the BSA and rivaroxaban complex at higher temperatures. The data of number of binding sites showed uniformity. The site marker experiments indicated site I (sub-domain IIA) as the principal site for rivaroxaban binding. The thermodynamic study experiments were carried at the temperatures of 298/303/308 K. The ∆G0, ∆H0 and ∆S0 at these temperatures ranged between − 24.67 and − 21.27 kJ mol−1 and the values for ∆H0 and ∆S0 were found to be − 126 kJ mol−1 and ∆S − 340 J mol−1 K−1 The negative value of ∆G0 indicating spontaneous binding between the two molecules. The negative values in ∆H0 and ∆S0 indicated van der Waals interaction and hydrogen bonding were involved during the interaction between rivaroxaban and BSA. The results of molecular docking were consistent with the results obtained from spectroscopic studies in establishing the principal binding site and type of bonds between rivaroxaban and BSA.

Naquotinib (ASP8273, NQT) is a novel third-generation epidermal growth factor receptor tyrosine kinase inhibitor (EGFR-TKIs). NQT was found to be more effective than osimertinib against the EGFR L858R plus T790M mutation (L858R+T790M). A rapid resolution liquid chromatography (RRLC)-tandem mass spectrometry (MS/MS) method was developed and validated for NQT quantification and its metabolic stability was investigated. NQT and foretinib (FTB) as an internal standard (IS) were separated using a mobile phase under isocratic conditions with a C18 column (reversed phase system). The linearity of the analytical method ranged from 5 to 500 ng mL⁻¹ (coefficient of correlation [r²] ≥ 0.9999) in a human liver microsome (HLM) matrix. The limit of detection and limit of quantification were 0.78 and 2.36 ng mL⁻¹, respectively. The inter-day and intra-day accuracy and precision were −6.36 to 1.88 and 0.99 to 2.58%, respectively. The metabolic stability of NQT in the HLM matrix was calculated using the in vitro half-life (t_1/2, 67.96 min) and intrinsic clearance (Cl_int, 2.12 mL min⁻¹ kg⁻¹). NQT is considered to be a moderate extraction ratio drug that is moderately excreted from the human body compared with other related TKIs. This proposed methodology is thought to be the first method for assessing NQT concentration and its metabolic stability.

Pemigatinib (PMB) is a small molecule inhibitor of fibroblast growth factor receptor 1 (FGFR1), FGFR2 and FGFR3. On April 17, 2020, the US Food and Drug Administration granted accelerated approval for PMB for the treatment of adults with previously treated, unresectable metastatic or locally advanced cholangiocarcinoma with a fibroblast growth factor receptor 2 (FGFR2) fusion or other rearrangement. PMB is considered the first targeted treatment for cholangiocarcinoma approved in the US. In this study, in silico prediction of PMB metabolic stability was done using the WhichP450 module of the StarDrop software package. Further, an LC-MS/MS analytical method was developed for PMB quantification in human liver microsomes (HLM) to experimentally assess metabolic stability. PMB and flavopiridol (FVL), used as an internal standard IS, were resolved using an isocratic mobile phase and a C18 stationary phase. The LC-MS/MS method showed linearity in the range of 5 to 500 ng mL⁻¹ in an HLM matrix (R² = 0.9995). The lower limit of quantification (LLOQ) was 5 ng mL⁻¹, indicating sensitivity. The inter- and intra-day accuracy and precision were within a variability of 10, confirming the reproducibility of the method. The measured in vitro half-life and intrinsic clearance of PMB were 27.29 min and 25.40 μL min⁻¹ mg⁻¹, respectively. PMB showed a moderate extraction ratio suggesting good bioavailability. The developed analytical method is the first LC-MS/MS method specific for PMB quantification with application to metabolic stability assessment.

Acyclovir (ACV) and penciclovir (PNV) have been commonly used during the last few decades as potent antiviral agents, especially for the treatment of herpes virus infections. In the present research their binding properties with human serum albumin (HSA) were studied using different advanced spectroscopic and in-silico methods. The interactions between ACV/PNV and HSA at the three investigated temperatures revealed a static type of binding. Extraction of the thermodynamic parameters of the ACV-HSA and PNV-HSA systems from the measured spectrofluorimetric data demonstrated spontaneous interactions with an enthalpy change (∆H⁰) of −1.79 ± 0.29 and −4.47 ± 0.51 kJ·mol⁻¹ for ACV and PNV, respectively. The entropy change (∆S⁰) of 79.40 ± 0.95 and 69.95 ± 1.69 J·mol⁻¹·K⁻¹ for ACV and PNV, respectively, hence supported a potential contribution of electrostatic binding forces to the ACV-HSA and PNV-HSA systems. Putative binding of ACV/PNV to HSA, using previously reported site markers, showed that ACV/PNV were bound to HSA within subdomains IIA and IIIA (Sudlow sites I and II). Further confirmation was obtained through molecular docking studies of ACV-HSA and PNV-HSA binding, which confirmed the binding site of ACV/PNV with the most stable configurations of ACV/PNV within the HSA. These ACV/PNV conformers were shown to have free energies of −25.61 and −22.01 kJ·mol⁻¹ for ACV within the HSA sites I and II and −22.97 and −26.53 kJ·mol⁻¹ for PNV in HSA sites I and II, with hydrogen bonding and electrostatic forces being the main binding forces in such conformers.