Candida albicans chemical structure

The gross structure of 73 was determined by a combination of spectroscopic and chemical means (112) stereochemistry was proved by single-crystal X-ray diffraction (113). Much later, 73 was also found in C. guianensis from Brazil (114). It was characterized by PMR and CMR data as well as by X-ray analysis. Gerrardine showed activity against Salmonella spp. (115), Candida albicans T.A., Escherichia coli, and Klebsiella pneumoniae D.T. (114). 

Bhandari et al. (56) modified a hit structure derived from the primary screening of various libraries (>300,000 compounds) on the zinc metalloenzyme phosphomannose isomerase from the yeast Candida albicans (CaPMI) to find enzyme inhibitors as jxitential antifungal agents. During primary screening only a 1296-member SP dipeptide pool library (Lll, Fig. 9.16) showed activity on the enzyme. Its deconvolution and analytical characterization led to the discovery of a by-product, derived from incomplete coupling, that showed activity on the enzyme. This compound (9.21, Fig. 9.16) showed a weak inhibitory activity on CaPMI (ICso = 40 xM) and was selected for further chemical profiling. 

In 1965, an important modification of the chemical structure of bakers yeast mannan was made by Ballou and his co-workers. They pointed out that the longest branching moieties of this mannan correspond to a tetraose, 0-orD-mannopyranosyl (1 - 3) 0-(x-D-mannopyranosyl (1- 2) O-oc-o-mannopyranosyl (l->2) mannose (23). In 1967, the Canadian workers and Hasenclever published the modified findings of structural analysis of the mannan of several Candida strains including those of C. albicans serotype A, C. albicans serotype B, C. tropicalis, C. stellatoidea, and C. parapsilosis, affording evidence that all mannans contain small amounts of al->3 linked D-mannopyranosyl residues in addition to the large amounts of al->2 and ocl->6 linkages (24). ... 

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