Prevalence and incidence of type 2 diabetes Mellitus (T2DM) in children has been increased worldwide due to obesity, lack of physical activity, improper diet, and family medical history. Other associated complications such as cardiovascular problems, dyslipidemia, hypertension, nonalcoholic fatty liver disease, pancreatic problems, pulmonary problems, and renal injury are found to attribute the ill-effects of T2DM complication in Pediatric population. Woefully, T2DM and its complications in the Pediatric population remain largely under studied and left untreated at time.

The increasing knowledge about the hepatitis C virus (HCV) gives rise to the development of novel and promising antiviral therapies. Despite apparent advances in this field, the common inhibitor of the NS3/4A protease from all HCV genotypes has not been designed yet. The main cause of the lack of such an inhibitor are sequential and structural differences among NS3/4A protease variants from existing HCV subtypes. This article presents differences and similarities in the structure and substrate specificity of selected enzyme isoforms, which may help to synthesise a specific inhibitor against all of them. The analysis performed by the authors showed that the identity of RNA sequences encoding the NS3 proteins from these HCV subtypes ranges from 69 to 91% (73.4% on average) while the identity of corresponding amino acid sequences is much higher and ranges from 80 to 95% (85.5% on average). Despite some differences between the peptide cofactors (NS4A) of the proteases from the selected HCV genotypes, their structure is similar and the sequence identity of genes encoding the NS4A peptides from the selected HCV genotypes ranges from 59% to 91% (77.7% on average). The alignment of amino acid sequences of the NS4A peptide variants revealed that its middle fragment, which is linked to the NS3 protein, is the least conserved region. The knowledge of differences in the structure of substrate binding pockets of the NS3/4A protease isoforms, affecting the strength of interactions with the substrates and inhibitors, will help to design the universal inhibitor of these enzymes.

A rapid, specific and economic UV spectrophotometric method has been developed using water as solvent to determine the tenofovir content in bulk and pharmaceutical dosage formulations. At a pre-determined λ max of 260 nm, it was proved linear in the range of 10-60 µg/ml and exhibited good correlation coefficient (0.0206 and 0.9808) and excellent mean recovery (99.00-00.07%). This method was successfully applied to the determination of tenofovir content in marketed brands from India and the results were in good agreement with the label claim. The method was validated statistically and by recovery studies for linearity, precision, repeatability, and reproducibility. The obtained results proved that the method can be employed for the routine analysis of tenofovir in bulks as well as in the commercial formulations.