@article { ISI:000248203200019,
	title = {Synthesis and evaluation of 1-deoxy-8-epi-castanospermine, 1-deoxy-8-hydroxymethyl castanospermine, and (6S,7S,8R,8aR)-8-amino-octahydroindolizine-6,7-diol},
	journal = {Tetrahedron},
	volume = {63},
	number = {22},
	year = {2007},
	month = {MAY},
	pages = {4756-4761},
	publisher = {PERGAMON-ELSEVIER SCIENCE LTD},
	type = {Article},
	address = {THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLAND},
	abstract = {<p>A short, versatile, and enantioselective synthesis of 1-deoxy-8-epi-castanospermine (5), 1-deoxy-8-hydroxymethyl castanospermine (6), and (6S,7S,8R,8aR)-8-amino-octahydroindolizine-6,7-diol (7) is achieved from a common template 12. The key step utilized is PET provoked amine radical cyclization of 11 to 12 in excellent diastereoselectivity. The exocyclic double bond at C-8 of the template is functionalized to obtain 5-7 as exclusive diastereomers. 1-Deoxy-8-epi-castanospermine exhibited inhibition of alpha- and beta-galactosidase and beta-glucosidase. Compounds 6 and 7 were found to be weak inhibitors of beta-glucosidase. (C) 2007 Elsevier Ltd. All rights reserved.</p>},
	keywords = {1-deoxy-8-epi-castanospermine, castanospermine, Glycosidase inhibitors},
	issn = {0040-4020},
	doi = {10.1016/j.tet.2007.03.085},
	author = {Pandey, Ganesh and Dumbre, Shrinivas G. and Pal, Sujit and Khan, Mohammad Islam and Shabab, A.}
}
@article { ISI:000272134300006,
	title = {Interaction of alpha-mannosidase from aspergillus fischeri with glycosidase inhibitors, metal ions and group specific reagents},
	journal = {Research Journal of Biotechnology},
	volume = {4},
	number = {4},
	year = {2009},
	month = {NOV},
	pages = {39-48},
	publisher = {RESEARCH JOURNAL BIOTECHNOLOGY},
	address = {SECTOR A-80, SCHEME NO 54, VIJAY NAGAR, A B ROAD, INDORE, 452 010 MP, INDIA},
	abstract = {<p>As an initial step towards using alpha-mannosidase as a target against anticancer drugs, inhibition studies of a model enzyme, class II alpha-mannosidase from Aspergillus fischeri in presence of polyhydroxy piperidine derived glycosidase inhibitors, metal ions and amino acid specific reagents were carried out to reveal the sensitivity of the enzyme. Three of the derivatives (Compound 20, 32 and 39)(11) showed competitive inhibition (K(i) =45, 48 and 235 mu M) and the binding of the inhibitors to the enzyme was entropically driven. Among the metal ions checked, Cu(++) (K(i) = 21nm) and Se(++) ions (K(i) = 32 mu M) showed noncompetitive and Co(++) (K(i) = 1.195 mM) showed competitive inhibition of the enzyme activity with insignificant change in the secondary structure of the protein. The above studies exhibit the Potential of the enzyme in studying anticancer drugs. Treatment of the enzyme with group specific reagents showed the presence of carboxylate, Arg and Cys at the active site. Substrate protection studies and kinetics of the modified enzyme confirmed the above results. Trp and His at the active site were observed to be in proximity.</p>},
	keywords = {active-site, alpha-Mannosidase, Chemical modification, Glycosidase inhibitors, metal ions},
	issn = {0973-6263},
	author = {Shashidhara, K. S. and Gaikwad, S. M. and Khan, Mohammad Islam and Bharadwaj, Kishor Chandra and Pandey, G.}
}
