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Abstract The present research evaluated the anti urolithic potential of Cyperus rotundus tubers extract using in silico, in vitro and in vivo techniques. In silicostudy was performed of Cyperus rotundus constituents and pathological protein oxalate oxidase (PDB Id: 2ETE). In vitrostudy, nucleation and aggregation assay involved for assessment of ethanol extract of Cyperus rotundus tuber (50-3000 µg/ml).In vivo studies involved that the Cyperus rotundusethanolic extract (100, 200 and 400 mg/kg B.wt.) wastreatedonsodium oxalate induced urolithiatic rats for seven days,evaluated kidney function by urine and serum biochemical analysis and statistical analysis performed usingGraphPad prism5 software.In silico results showedthat Cyperus rotundus constituents,Humulene epoxide, 4-Oxo-alpha-ylangene, Cubebol were exhibited better binding energyonoxalate oxidase.Ethanolic extract of Cyperus rotundustuber was exhibited nucleation, aggregation of calcium oxalate monohydrate crystals inhibition in dosedependent manner. Sodium oxalate treatment was triggered biochemical changesin the urine that have been substantially prevented by the ethanolic extract of Cyperus rotundus tuber. The current findings Cyperus rotundus anti urolithic activity due to antioxidant essential oils. The molecular docking results could be used to optimize lead and develop the appropriate urolithiasis treatment.

Abstract: The influence of Escherichia coliform (E. coli), especially the proteins it secretes, on the nucleation, growth and aggregation processes of calcium bilirubinate (CaBR) in different mimic systems, such as NaCl aqueous solution and model bile, is studied in this paper. The results show that in NaCl aqueous solution the morphology of calcium bilirubinate (CaBR) changes from amorphous sheet structure to a highly self-organized and highly self-replicated fractal structure that is accumulated by rhombic microcrystals after the addition of E. coli. In model bile with the existence of E. coli, CaBR also forms a fractal structure, but the fractal structure is staghorn-like. Meanwhile, the composition of the prepared CaBRs is nonstoichiometric, and the crystallization is greatly improved with the existence of E. coli. Besides, formation mechanism of CaBRs affected by E. coli is explored, showing that the proteins secreted by E. coli interact with the Ca2+ ions to provide nucleation sites for CaBRs, and the conformation of the proteins becomes more ordered, resulting in the improvement of the crystalline of CaBRs. On the other hand, the interaction of proteins and the Ca2+ ions also promote the aggregation state of the CaBRs. [Copyright &y& Elsevier]