@article { ISI:000231712000007, title = {Synthesis of bile acid dimers linked with 1,2,3-triazole ring at C-3, C-11, and C-24 positions}, journal = {Synlett}, number = {14}, year = {2005}, month = {SEP}, pages = {2155-2158}, publisher = {GEORG THIEME VERLAG KG}, type = {Article}, address = {RUDIGERSTR 14, D-70469 STUTTGART, GERMANY}, abstract = {

1,3-Dipolar cycloaddition of propargyl ester of a bile acid to an azide group attached at different positions of another bile acid gave three new 1,2,3-triazole-containing dimeric analogues in excellent yields.

}, keywords = {1, 2, 3-dipolar cycloaddition, 3-Triazole, Bile acids, Click chemistry, steroidal dimers}, issn = {0936-5214}, doi = {10.1055/s-2005-872223}, author = {Aher, Nilkanth G. and Pore, VS} } @article {KULKARNI, title = {Polymer supported vanadium and molybdenum complexes as potential catalysts for the oxidation and oxidative bromination of organic substrates}, journal = {Dalton Transactions}, number = {29}, year = {2006}, note = {Conference on Atomic Molecular and Optical Physics, Calcutta, INDIA, DEC 13-15, 2005}, month = {APR}, pages = {3561-3575}, publisher = {Indian Assoc Cultivat Sci}, type = {Review}, address = {PO BOX 128 FARRER RD, SINGAPORE 9128, SINGAPORE}, abstract = {

{The Schiff base (H(2)fsal-ohyba) derived from 3-formylsalicylic acid and o-hydroxybenzylamine has been covalently bonded to chloromethylated polystyrene cross-linked with 5\% divinylbenzene ( abbreviated as PS-H(2)fsal-ohyba, I). Treatment of [

}, keywords = {Bile acids, bis-steroids, hybrids, Peptides, polyamines, saponins, steroidal conjugates, synthetic ionophores}, doi = {10.1039/b600822d}, author = {Maurya, Mannar R. and Kumar, Umesh and Manikandan, Palanichamy} } @article { ISI:000361004700026, title = {Design and synthesis of 11 alpha-substituted bile acid derivatives as potential anti-tuberculosis agents}, journal = {Bioorganic \& Medicinal Chemistry Letters}, volume = {25}, number = {19}, year = {2015}, month = {OCT}, pages = {4185-4190}, publisher = {PERGAMON-ELSEVIER SCIENCE LTD}, address = {THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLAND}, abstract = {

We have synthesized a series of novel 11 alpha-triazoyl bile acid derivatives. In addition, we also have synthesized N-alkyl and N-acyl derivatives of C-11 amino bile acid esters. All the compounds were evaluated for the inhibitory activity against Mycobacterium tuberculosis H37Ra (MTB) at 30 mu g/mL level. Four lead compounds (2b, 3, 7 and 8) were further confirmed from their dose dependent effect against MTB. These compounds were found to be active against Dormant and active stage MTB under both in vitro as well as within THP1 host macrophages. The most promising compound 2b showed strong antitubercular activities against MTB under in vitro and ex vivo (IC90 value of similar to 3 mu g/mL) conditions and almost insignificant cytotoxicity up to 100 mu g/mL against THP-1, A549 and PANC-1 human cancer cell lines. Inactivity of all these compounds against Gram positive and Gram negative bacteria indicates their specificity. Molecular docking studies of these compounds into the active site of DprE1 enzyme revealed a similar binding mode to native ligands in the crystal structure thereby helping to establish a structural basis of inhibition of MTB. The synthesized compounds were analyzed for ADME properties and showed potential to develop good oral drug candidates. Our results clearly indicate the identification of some novel, selective and specific inhibitors against MTB that can be explored further for potential antitubercular drug. (C) 2015 Elsevier Ltd. All rights reserved.

}, keywords = {Antituberculosis, Bile acids, Cycloaddition, Docking study, In silico ADME}, issn = {0960-894X}, doi = {10.1016/j.bmcl.2015.08.006}, author = {Pore, Vandana S. and Divse, Jaisingh M. and Charolkar, Chaitanya R. and Nawale, Laxman U. and Khedkar, Vijay M. and Sarkar, Dhiman} } @article { ISI:000370100200012, title = {Highly active bile salt hydrolase from enterococcus faecalis shows positive cooperative kinetics}, journal = {Process Biochemistry}, volume = {51}, number = {2}, year = {2016}, month = {FEB}, pages = {263-269}, publisher = {ELSEVIER SCI LTD}, address = {THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLAND}, abstract = {

Bile salt hydrolase (BSH; cholylglycine hydrolase, EC 3.5.1.24) is an important enzyme that catalyses the deconjugation of bile acids conjugated with glycine or taurine and assists in the reduction of blood cholesterol levels. In the present study, we report the cloning, overexpression and characterisation of BSH gene from a gut-associated microbe Enterococcus faecalis (EfBSH). The overexpressed protein in Escherichia coli was purified to homogeneity. Optimum pH and temperature for activity were found to be 5.0 and 50 degrees C, respectively. The enzyme was considerably stable in the pH range of 5.0-7.0 and at a temperature of up to 50 degrees C. It showed high specific activity of 1390 U mg(-1) and 1289 U mg-1 for substrates such as glycocholic acid (GCA) and glycodeoxycholic acid (GDCA), respectively. The effect of additives on enzyme activity was assessed, and the detergent Triton X showed a marginally enhanced activity. The enzyme demonstrated unique enzyme kinetics of non-linear regression, thereby displaying positive cooperativity. In addition, the modulating effect of the non-substrate ligand Pen V on the hydrolysing ability of EfBSH towards bile acid such as GDCA was measured. It was observed that Pen V significantly enhanced the BSH activity. This is markedly different from the previously reported competitive inhibition of BSH activity by Pen V. (C) 2015 Elsevier Ltd. All rights reserved.

}, keywords = {Allosteric regulation, Bile acids, Bile salt hydrolase, Enzyme kinetics, Gut organism, Penicillin V acylase}, issn = {1359-5113}, doi = {10.1016/j.procbio.2015.12.006}, author = {Chand, Deepak and Ramasamy, Sureshkumar and Suresh, C. G.} }