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A series of seventeen analogs (1─17) were synthesized and characterized through different spectroscopic techniques such as 1H, 13CNMR, HR-EI-MS and were evaluated for in vitro thymidine phosphorylase inhibition. All compounds showed excellent to good thymidine phosphorylase activity having IC50 value ranging between 4.10 ± 0.20 and 54.60 ± 1.40 µM when compared with standard drug 7-deazaxanthine (IC50 = 38.68 ± 1.12 µM). Among the series, compounds 1 (IC50 = 8.30 ± 0.30 µM), 6 (IC50 = 6.30 ± 0.10 µM), 11 (IC50 = 8.40 ± 0.30 µM) and 16 (IC50 = 4.10 ± 0.20 µM) were found more potent. Potent compounds were further subjected to molecular docking study to identify their interactions with the active site of amino acid. Structure activity relationship was done for all analogs mostly based on substitution pattern on phenyl and isatin rings.

We have synthesized nineteen (1–19) bisindolylmethane sulfonamide analogs, characterized by different spectroscopic techniques such as 1HNMR and EI-MS and tested for α-amylase inhibitory potential. All compounds showed excellent to moderate degree of α-amylase inhibitory potential with IC50 values ranging between 1.192 ± 0.51 to 3.057 ± 0.18 μM as equated with standard acarbose (IC50 values 0.83 ± 0.36 μM). Among the series, six analogs such as 1, 4, 5, 6, 10, and 14 showed potent α-amylase inhibition with IC50 values 1.747 ± 0.2, 1.208 ± 0.15, 1.192 ± 0.51, 1.858 ± 0.08, 1.358 ± 0.27 and 1.527 ± 0.17 μM, respectively, as equated with standard acarbose. The structure-activity relationship based upon different substituents on phenyl part. Molecular docking studies performed to recognize the binding interaction of the most active compounds.

Five organotin complexes have been derived from a Schiff base, 2-[(4-dimethylamino-benzylidene)amino] phenol. The synthesis of target compounds is confirmed by spectroscopic techniques: IR, 1H NMR, and 13C NMR. Activity of the initial Schiff base and its complexes has been tested with respect to various bacterial strains, and the results obtained are quite promising against both Gram-positive and Gram-negative bacteria.

Retinitis punctata albescens (RPA) is an ocular disease characterized by decreased visual acuity, night blindness, atropic maculopathy, and pigmentary retinopathy. Multiple genes have been linked to the etiology of RPA. In this study, we investigated the genetic causes of RPA in a consanguineous Pakistani family with multiple affected individuals. We performed whole-exome sequencing of seven family members, and screened variants co-segregating with RPA in recessive fashion. Bioinformatic and in silico analyses revealed that all affected individuals were homozygous for a novel mutation that substitutes glycine with arginine at position 66 (c.196 G>C) in exon 2 of the lecithin retinol acyltransferase (LRAT) that converts all-trans retinol to 11-cis retinal in the retinal pigment epithelium. This mutation was not present in 217 unrelated Pakistani control subjects nor in the Exome Aggregation Consortium database containing exome data from 60,638 individuals worldwide. Mutations in the LRAT gene were previously found from the patients with Leber congenital amaurosis and retinal dystrophy, however, we report first time that disruptions in this gene are also associated with RPA.

Compounds 1–30 showed varying degree of α-glucosidase inhibition with IC50 values ranging between 187 and 420 μM. Compounds 1, 2, 3, 6, 8, 12, and 4 (IC50 = 187.7 ± 3.05, 203.4 ± 4.0, 240.7 ± 1.9, 252.9 ± 3.9, 285.2 ± 6.3, 399.07 ± 1.2, and 420.36 ± 5.6 μM, respectively) were found to be more active than standard acarbose (IC50 = 906 ± 6.3 μM). The synthetic compounds were also tested for urease inhibition. Compounds 5 (IC50 = 19.6 ± 1.0 μM) and 1 (IC50 = 21.6 ± 0.6 μM) showed better activity than standard drug thiourea (IC50 = 21.8 ± 1.6 μM). The crystal structures of compounds 15 and 16 are also reported. Compounds 1−30 synthesized and evaulated for Alpha-glucosidase as well as Ureas inhibition. The crystal structures of compounds 15 and 16 are also reported

Pyridyl-benzimidazole analogues 1–11 with variable substituent on phenyl ring of phenacyl moiety were synthesized and evaluated for their urease inhibitory activity. The compounds exhibited urease inhibition with IC50 between 19.22 and 77.31 µM. Compounds 4 (IC50 = 19.22 ± 0.49 µM) showed a urease inhibition comparable to thiourea (IC50 = 21.00 ± 0.01 µM) and twofold more active than acetohydroxamic acid (IC50 = 42.00 ± 1.26 µM) (standards), respectively. Moreover, compounds 5 (IC50 = 21.55 ± 0.36 µM), 1 (IC50 = 24.37 ± 0.41 µM), 7 (IC50 = 25.44 ± 0.19 µM), 6 (IC50 = 27.62 ± 0.25 µM), 3 (IC50 = 31.32 ± 0.75 µM), 8 (40.88 ± 0.36 µM) and 9 (41.22 ± 0.42 µM) also exhibited excellent activities when compared to the standards. Compounds 2 (IC50 = 65.46 ± 0.75 µM), 10 (68.99 ± 0.33 µM) and 11 (77.31 ± 0.51 µM) showed a moderate activity. The size of the substituents and their electron donating or withdrawing affects as well as their position on phenyl apparently modulates the enzyme inhibitory activity.

Some new transition metal complexes with monomethyl succinate are reported. Several physical techniques, such as elemental analysis and melting point, and in addition various spectroscopic techniques including 1H-, 13C-NMR and UV/visible and infrared spectroscopy were used to study the chemical structure of the prepared complexes. The octahedral geometry is proposed on the basis of these spectral techniques. The synthesized complexes were also exposed to various bacteria and fungi to establish their bioactivities.

Treatment of indole with substituted aldehyde in the presence of equimolar amount of sodium bromate and sodium hydrogen sulfite mixture in water yielded corresponding substituted bis(indolyl)methanes in good yields. This provides a facile and environmentally friendly method towards the synthesis of an important class of organic compounds.