@article { ISI:000237886100006,
	title = {Convenient chemoenzymatic synthesis of (1S,7aS)-1-hydroxy-5-oxo-4-(2 {\textquoteleft}-carboxyethyl)-7a-methyltetrahydro-indane - a key intermediate of steroids},
	journal = {Journal of Molecular Catalysis B-Enzymatic},
	volume = {40},
	number = {1-2},
	year = {2006},
	month = {MAY},
	pages = {38-43},
	publisher = {ELSEVIER SCIENCE BV},
	type = {Article},
	address = {PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS},
	abstract = {<p>A porcine pancreatic lipase mediated enzymatic hydrolysis of (+/-)-1-acetoxy-5-oxo-4-(2 {\textquoteleft}-carbomethoxyethyl)-7a-methyltetrahydroindane (5b) furnished (1S,7aS)-1-acetoxy-5-oxo-4-(2 {\textquoteleft}-carbomethoxyethyl)-7a-methyltetrahydro-indane (9) and (1R,7aR)-1-hydroxy-5-oxo-4-(2 {\textquoteleft}-carbomethoxyethyl)-7a-methyltetrahydro-indane (8) with \&gt; 99\% e.e. which on further chemical hydrolysis gave 1 and ent-1, key intermediates of steroids. (c) 2006 Elsevier B.V. All rights reserved.</p>},
	keywords = {chemoenzymatic method, Enzymatic hydrolysis, steroids, terpenoids},
	issn = {1381-1177},
	doi = {10.1016/j.molcatb.2006.01.037},
	author = {Kalkote, Uttam R. and Purude, A. N. and Puranik, Vedavati G. and Gurjar, M. K.}
}
@article {46046,
	title = {Steroidal thiazolidinone derivatives: design, synthesis and their molecular interaction with human serum albumin},
	journal = {Steroids},
	volume = {148},
	year = {2019},
	month = {AUG},
	pages = {99-113},
	type = {Article},
	abstract = {<p>A series of steroidal thiazolidinone derivatives have been synthesized through one-pot multicomponent reaction involving steroidal ketone, thiosemicarbazide/methyl-thiosemicarbazide and DMAD in presence of AlCl3 as a Lewis acid catalyst. Among all the synthesized steroidal thiazolidinone derivatives, compound 7-9 (ST 7-9) were investigated for their in vitro molecular interaction with human serum albumin. Intrinsic fluorescence spectroscopy, constant wavelength synchronous fluorescence spectroscopy, circular dichroism and UV-visible absorption techniques have been exploited to characterize the binding phenomena in phosphate buffer solution at pH 7.4. The experimental results indicated that ST 7-9 bind to HSA and the intrinsic fluorescence of HSA was quenched through static quenching mechanism. The binding parameters were calculated and the binding constants obtained were 1.44 x 10(5) M-1 for ST 7, 0.84 x 10(5) M-1 for ST 8 and 1.06 x 10(5) M-1 for ST 9. Circular dichroism analysis confirms that the presence of ST 7-9, altered the secondary structure of HSA due to partial unfolding of the polypeptide chain. Furthermore, hemolytic activity assay demonstrated that the synthesized steroidal thiazolidinone derivatives have good compatibility towards human red blood cells. Finally, molecular docking studies revealed that the steroidal thiazolidinones can bind in the hydrophobic cavity of HSA, by hydrophobic and hydrogen bonding interaction. These results provided valuable information about the binding mechanism of ST 7-9 with HSA and play a pivotal role in the development of steroidal heterocycle inspired compounds.</p>
},
	keywords = {heterocycles, Human serum albumin, steroids, Thiazolidinone},
	issn = {0039-128X},
	doi = {10.1016/j.steroids.2019.02.015},
	author = {Ansari, Anam and Ali, Abad and Asif, Mohd and Shamsuzzaman}
}
