Dutta S

References (15)

Title : Prediction of matrilineal specific patatin-like protein governing in-vivo maternal haploid induction in maize using support vector machine and di-peptide composition - Dutta_2024_Amino.Acids_56_20
Author(s) : Dutta S , Zunjare RU , Sil A , Mishra DC , Arora A , Gain N , Chand G , Chhabra R , Muthusamy V , Hossain F
Ref : Amino Acids , 56 :20 , 2024
Abstract : The mutant matrilineal (mtl) gene encoding patatin-like phospholipase activity is involved in in-vivo maternal haploid induction in maize. Doubling of chromosomes in haploids by colchicine treatment leads to complete fixation of inbreds in just one generation compared to 6-7 generations of selfing. Thus, knowledge of patatin-like proteins in other crops assumes great significance for in-vivo haploid induction. So far, no online tool is available that can classify unknown proteins into patatin-like proteins. Here, we aimed to optimize a machine learning-based algorithm to predict the patatin-like phospholipase activity of unknown proteins. Four different kernels [radial basis function (RBF), sigmoid, polynomial, and linear] were used for building support vector machine (SVM) classifiers using six different sequence-based compositional features (AAC, DPC, GDPC, CTDC, CTDT, and GAAC). A total of 1170 protein sequences including both patatin-like (585 sequences) from various monocots, dicots, and microbes; and non-patatin-like proteins (585 sequences) from different subspecies of Zea mays were analyzed. RBF and polynomial kernels were quite promising in the prediction of patatin-like proteins. Among six sequence-based compositional features, di-peptide composition attained > 90% prediction accuracies using RBF and polynomial kernels. Using mutual information, most explaining dipeptides that contributed the highest to the prediction process were identified. The knowledge generated in this study can be utilized in other crops prior to the initiation of any experiment. The developed SVM model opened a new paradigm for scientists working in in-vivo haploid induction in commercial crops. This is the first report of machine learning of the identification of proteins with patatin-like activity.
ESTHER : Dutta_2024_Amino.Acids_56_20
PubMedSearch : Dutta_2024_Amino.Acids_56_20
PubMedID: 38460024

Title : Degradation of complex arabinoxylans by human colonic Bacteroidetes - Pereira_2021_Nat.Commun_12_459
Author(s) : Pereira GV , Abdel-Hamid AM , Dutta S , D'Alessandro-Gabazza CN , Wefers D , Farris JA , Bajaj S , Wawrzak Z , Atomi H , Mackie RI , Gabazza EC , Shukla D , Koropatkin NM , Cann I
Ref : Nat Commun , 12 :459 , 2021
Abstract : Some Bacteroidetes and other human colonic bacteria can degrade arabinoxylans, common polysaccharides found in dietary fiber. Previous work has identified gene clusters (polysaccharide-utilization loci, PULs) for degradation of simple arabinoxylans. However, the degradation of complex arabinoxylans (containing side chains such as ferulic acid, a phenolic compound) is poorly understood. Here, we identify a PUL that encodes multiple esterases for degradation of complex arabinoxylans in Bacteroides species. The PUL is specifically upregulated in the presence of complex arabinoxylans. We characterize some of the esterases biochemically and structurally, and show that they release ferulic acid from complex arabinoxylans. Growth of four different colonic Bacteroidetes members, including Bacteroides intestinalis, on complex arabinoxylans results in accumulation of ferulic acid, a compound known to have antioxidative and immunomodulatory properties.
ESTHER : Pereira_2021_Nat.Commun_12_459
PubMedSearch : Pereira_2021_Nat.Commun_12_459
PubMedID: 33469030
Gene_locus related to this paper: 9bace-k9e1w0 , 9bace-b3c976 , 9bace-e2ncy6 , 9bace-e2ncy7 , 9bace-a0a380yku1 , 9bace-b3c969 , 9bace-b3c974 , 9bace-b3c975

Title : Enzyme leaps fuel antichemotaxis - Jee_2018_Proc.Natl.Acad.Sci.U.S.A_115_14
Author(s) : Jee AY , Dutta S , Cho YK , Tlusty T , Granick S
Ref : Proc Natl Acad Sci U S A , 115 :14 , 2018
Abstract : There is mounting evidence that enzyme diffusivity is enhanced when the enzyme is catalytically active. Here, using superresolution microscopy [stimulated emission-depletion fluorescence correlation spectroscopy (STED-FCS)], we show that active enzymes migrate spontaneously in the direction of lower substrate concentration ("antichemotaxis") by a process analogous to the run-and-tumble foraging strategy of swimming microorganisms and our theory quantifies the mechanism. The two enzymes studied, urease and acetylcholinesterase, display two families of transit times through subdiffraction-sized focus spots, a diffusive mode and a ballistic mode, and the latter transit time is close to the inverse rate of catalytic turnover. This biochemical information-processing algorithm may be useful to design synthetic self-propelled swimmers and nanoparticles relevant to active materials. Executed by molecules lacking the decision-making circuitry of microorganisms, antichemotaxis by this run-and-tumble process offers the biological function to homogenize product concentration, which could be significant in situations when the reactant concentration varies from spot to spot.
ESTHER : Jee_2018_Proc.Natl.Acad.Sci.U.S.A_115_14
PubMedSearch : Jee_2018_Proc.Natl.Acad.Sci.U.S.A_115_14
PubMedID: 29255047

Title : Effect of pesticide exposure on the cholinesterase activity of the occupationally exposed tea garden workers of Northern part of West Bengal, India - Dutta_2018_Biomarkers__1
Author(s) : Dutta S , Bahadur M
Ref : Biomarkers , :1 , 2018
Abstract : CONTEXT: Pesticide poisoning and related deaths is a global concern, but there is little information about its effect on the occupationally exposed tea garden workers of North Bengal. OBJECTIVE: This study investigates the level of AChE and BuChE in the blood of the tea garden workers, at risk of exposure to a mixture of pesticides. MATERIALS AND METHODS: The study sample consisted of pesticide exposed workers, non exposed (control), smokers and alcoholics. AChE and BuChE activity was measured and tested for significance. RESULTS: Results showed that AChE activity was half in the pesticide-exposed individuals than controls (p </= 0.001). BuChE activity was also significantly decreased in the pesticide-exposed individuals than controls (p </= 0.001), while AChE and BuChE activity in smokers and alcoholics were not different from that of controls. However, significantly decreased AChE and BuChE activities were recorded in pesticide-exposed workers compared to smokers and alcoholics. CONCLUSION: The results indicated that the decrease in enzyme activities in tea garden workers was due to mixed pesticides (containing organophosphates) exposure. Age was not found to influence the enzyme activities. However, the gender had little effect on the enzyme activities but the effect was not so prominent.
ESTHER : Dutta_2018_Biomarkers__1
PubMedSearch : Dutta_2018_Biomarkers__1
PubMedID: 30512980

Title : Proteomic analysis to unravel the complex venom proteome of eastern India Naja naja: Correlation of venom composition with its biochemical and pharmacological properties - Dutta_2017_J.Proteomics_156_29
Author(s) : Dutta S , Chanda A , Kalita B , Islam T , Patra A , Mukherjee AK
Ref : J Proteomics , 156 :29 , 2017
Abstract : The complex venom proteome of the eastern India (EI) spectacled cobra (Naja naja) was analyzed using tandem mass spectrometry of cation-exchange venom fractions. About 75% of EI N. naja venom proteins were <18kDa and cationic at physiological pH of blood. SDS-PAGE (non-reduced) analysis indicated that in the native state venom proteins either interacted with each-other or self-aggregated resulting in the formation of higher molecular mass complexes. Proteomic analysis revealed that 43 enzymatic and non-enzymatic proteins in EI N. naja venom with a percent composition of about 28.4% and 71.6% respectively were distributed over 15 venom protein families. The three finger toxins (63.8%) and phospholipase A2s (11.4%) were the most abundant families of non-enzymatic and enzymatic proteins, respectively. nanoLC-ESI-MS/MS analysis demonstrated the occurrence of acetylcholinesterase, phosphodiesterase, cholinesterase and snake venom serine proteases in N. naja venom previously not detected by proteomic analysis. ATPase, ADPase, hyaluronidase, TAME, and BAEE-esterase activities were detected by biochemical analysis; however, due to a limitation in the protein database depository they were not identified in EI N. naja venom by proteomic analysis. The proteome composition of EI N. naja venom was well correlated with its in vitro and in vivo pharmacological properties in experimental animals and envenomed human. BIOLOGICAL SIGNIFICANCE: Proteomic analysis reveals the complex and diverse protein profile of EI N. naja venom which collectively contributes to the severe pathophysiological manifestation upon cobra envenomation. The study has also aided in comprehending the compositional variation in venom proteins of N. naja within the Indian sub-continent. In addition, this study has also identified several enzymes in EI N. naja venom which were previously uncharacterized by proteomic analysis of Naja venom.
ESTHER : Dutta_2017_J.Proteomics_156_29
PubMedSearch : Dutta_2017_J.Proteomics_156_29
PubMedID: 28062377

Title : Glial expression of Swiss cheese (SWS), the Drosophila orthologue of neuropathy target esterase (NTE), is required for neuronal ensheathment and function - Dutta_2016_Dis.Model.Mech_9_283
Author(s) : Dutta S , Rieche F , Eckl N , Duch C , Kretzschmar D
Ref : Dis Model Mech , 9 :283 , 2016
Abstract : Mutations in Drosophila Swiss cheese (SWS) or its vertebrate orthologue neuropathy target esterase (NTE), respectively, cause progressive neuronal degeneration in Drosophila and mice and a complex syndrome in humans that includes mental retardation, spastic paraplegia and blindness. SWS and NTE are widely expressed in neurons but can also be found in glia; however, their function in glia has, until now, remained unknown. We have used a knockdown approach to specifically address SWS function in glia and to probe for resulting neuronal dysfunctions. This revealed that loss of SWS in pseudocartridge glia causes the formation of multi-layered glial whorls in the lamina cortex, the first optic neuropil. This phenotype was rescued by the expression of SWS or NTE, suggesting that the glial function is conserved in the vertebrate protein. SWS was also found to be required for the glial wrapping of neurons by ensheathing glia, and its loss in glia caused axonal damage. We also detected severe locomotion deficits in glial sws-knockdown flies, which occurred as early as 2 days after eclosion and increased further with age. Utilizing the giant fibre system to test for underlying functional neuronal defects showed that the response latency to a stimulus was unchanged in knockdown flies compared to controls, but the reliability with which the neurons responded to increasing frequencies was reduced. This shows that the loss of SWS in glia impairs neuronal function, strongly suggesting that the loss of glial SWS plays an important role in the phenotypes observed in the sws mutant. It is therefore likely that changes in glia also contribute to the pathology observed in humans that carry mutations in NTE.
ESTHER : Dutta_2016_Dis.Model.Mech_9_283
PubMedSearch : Dutta_2016_Dis.Model.Mech_9_283
PubMedID: 26634819

Title : APOE-varepsilon4 Carrier Status and Donepezil Response in Patients with Alzheimer's Disease - Waring_2015_J.Alzheimers.Dis_47_137
Author(s) : Waring JF , Tang Q , Robieson WZ , King DP , Das U , Dubow J , Dutta S , Marek GJ , Gault LM
Ref : J Alzheimers Dis , 47 :137 , 2015
Abstract : BACKGROUND: Previous studies have investigated associations between apolipoprotein E (APOE)-varepsilon4 allele status and acetylcholinesterase inhibitor treatment response in patients with Alzheimer's disease. The ability to draw definitive conclusions regarding the effect of APOE-varepsilon4 genotype on treatment response has been hindered by inconsistent results among studies and methodological limitations that restrict interpretation of study findings. OBJECTIVE: To determine whether APOE-varepsilon4 carrier status influences the magnitude of change in 13-item Alzheimer's Disease Assessment Scale-Cognitive Subscale (ADAS-cog) score associated with acetylcholinesterase inhibitor treatment (i.e., donepezil).
METHODS: Analyses were performed using pooled data from the donepezil and placebo treatment arms of three consecutive, similarly designed, 12-week, multi-national, randomized clinical studies that enrolled patients with mild-to-moderate Alzheimer's disease. Correlations between APOE-varepsilon4 carrier status and ADAS-cog scores were evaluated using analysis of covariance.
RESULTS: No appreciable interaction between donepezil response and APOE-varepsilon4 carrier status or copy number was detected. Both carriers and non-carriers of APOE-varepsilon4 who received donepezil experienced significant improvements from baseline in ADAS-cog score versus placebo (p < 0.05). Change from baseline to final observation in the donepezil treatment group was - 2.95 for APOE-varepsilon4 carriers and - 4.09 for non-carriers (p = 0.23). In contrast, non-carriers of APOE-varepsilon4 in the placebo treatment group exhibited a greater improvement from baseline versus carriers (-2.38 versus - 0.60, p = 0.05). CONCLUSION: Within this population, APOE genotype had no statistically significant effect on cognitive response to donepezil treatment; however, APOE-varepsilon4 allele status was associated with a difference in the magnitude of the change in ADAS-cog of placebo-treated patients.
ESTHER : Waring_2015_J.Alzheimers.Dis_47_137
PubMedSearch : Waring_2015_J.Alzheimers.Dis_47_137
PubMedID: 26402762

Title : In vitro assessment of anticholinesterase and NADH oxidase inhibitory activities of an edible fern, Diplazium esculentum - Roy_2015_J.Basic.Clin.Physiol.Pharmacol_26_395
Author(s) : Roy S , Dutta S , Chaudhuri TK
Ref : J Basic Clin Physiol Pharmacol , 26 :395 , 2015
Abstract : BACKGROUND: Diplazium esculentum is the most commonly consumed edible fern throughout Asia and Oceania. Several studies have been performed so far to determine different functional properties of this plant, but there have been no reports on the anticholinesterase and nicotinamide adenine dinucleotide (NADH) oxidase inhibitory activities of this plant. Therefore, the present study was conducted to determine the anticholinesterase and NADH oxidase inhibitory activities of 70% methanolic extract of D. esculentum.
METHODS: The D. esculentum extract was investigated for its acetylcholinesterase and NADH oxidase inhibitory activities as well as its free radical scavenging and total antioxidant activities in the linoleic acid system. The free radical scavenging activity of the extract was determined by the 2,2-diphenyl-1-picryl-hydrazyl (DPPH) method. The total antioxidant activity of the extract was evaluated by ferric thiocyanate (FTC) and thiobarbituric acid (TBA) methods.
RESULTS: The D. esculentum extract inhibited acetylcholinesterase and NADH oxidase in a dose-dependent manner, with IC50 values of 272.97+/-19.38 and 265.81+/-21.20 mug/mL, respectively. The extract also showed a potent DPPH radical scavenging activity with an IC50 value of 402.88+/-12.70 mug/mL. Moreover, the extract showed 27.41% and 33.22% of total antioxidant activities determined by FTC and TBA methods, respectively.
CONCLUSIONS: Results indicated that 70% methanolic extract of D. esculentum effectively inhibited the enzymes acetylcholinesterase and NADH oxidase and acted as a potent antioxidant and free radical scavenger. These in vitro assays indicate that this plant extract is a significant source of natural antioxidants, which may be helpful in preventing the progression of various neurodegenerative disorders associated with oxidative stress.
ESTHER : Roy_2015_J.Basic.Clin.Physiol.Pharmacol_26_395
PubMedSearch : Roy_2015_J.Basic.Clin.Physiol.Pharmacol_26_395
PubMedID: 25719308

Title : Rat hormone sensitive lipase inhibition by cyclipostins and their analogs - Vasilieva_2015_Bioorg.Med.Chem_23_944
Author(s) : Vasilieva E , Dutta S , Malla RK , Martin BP , Spilling CD , Dupureur CM
Ref : Bioorganic & Medicinal Chemistry , 23 :944 , 2015
Abstract : Cyclipostins are bicyclic lipophilic phosphate natural products. We report here that synthesized individual diastereomers of cyclipostins P and R have nanomolar IC50s toward hormone sensitive lipase (HSL). The less potent diastereomers of these compounds have 10-fold weaker IC50s. The monocyclic phosphate analog of cyclipostin P is nearly as potent as the bicyclic natural product. Bicyclic phosphonate analogs of both cyclipostins exhibit IC50s similar to those of the weaker diastereomer phosphates (about 400nM). The monocyclic phosphonate analog of cyclipostin P has similar potency. A series of monocyclic phosphonate analogs in which a hydrophobic tail extends from the lactone side of the ring are considerably poorer inhibitors, with IC50s around 50muM. Finally cyclophostin, a related natural product inhibitor of acetylcholinesterase (AChE) that lacks the hydrocarbon tail of cyclipostins, is not active against HSL. These results indicate a critical SAR for these compounds, the hydrophobic tail. The smaller lactone ring is not critical to activity, a similarity shared with cyclophostin and AChE. The HSL kinetics of inhibition for the cyclipostin P trans diastereomer were examined in detail. The reaction is irreversible with a KI of 40nM and a rate constant for inactivation of 0.2min(-1). These results are similar to those observed for cyclophostin and AChE.
ESTHER : Vasilieva_2015_Bioorg.Med.Chem_23_944
PubMedSearch : Vasilieva_2015_Bioorg.Med.Chem_23_944
PubMedID: 25678014
Gene_locus related to this paper: ratno-hslip

Title : Structure of a modular polyketide synthase - Dutta_2014_Nature_510_512
Author(s) : Dutta S , Whicher JR , Hansen DA , Hale WA , Chemler JA , Congdon GR , Narayan AR , Hakansson K , Sherman DH , Smith JL , Skiniotis G
Ref : Nature , 510 :512 , 2014
Abstract : Polyketide natural products constitute a broad class of compounds with diverse structural features and biological activities. Their biosynthetic machinery, represented by type I polyketide synthases (PKSs), has an architecture in which successive modules catalyse two-carbon linear extensions and keto-group processing reactions on intermediates covalently tethered to carrier domains. Here we used electron cryo-microscopy to determine sub-nanometre-resolution three-dimensional reconstructions of a full-length PKS module from the bacterium Streptomyces venezuelae that revealed an unexpectedly different architecture compared to the homologous dimeric mammalian fatty acid synthase. A single reaction chamber provides access to all catalytic sites for the intramodule carrier domain. In contrast, the carrier from the preceding module uses a separate entrance outside the reaction chamber to deliver the upstream polyketide intermediate for subsequent extension and modification. This study reveals for the first time, to our knowledge, the structural basis for both intramodule and intermodule substrate transfer in polyketide synthases, and establishes a new model for molecular dissection of these multifunctional enzyme systems.
ESTHER : Dutta_2014_Nature_510_512
PubMedSearch : Dutta_2014_Nature_510_512
PubMedID: 24965652

Title : Structural rearrangements of a polyketide synthase module during its catalytic cycle - Whicher_2014_Nature_510_560
Author(s) : Whicher JR , Dutta S , Hansen DA , Hale WA , Chemler JA , Dosey AM , Narayan AR , Hakansson K , Sherman DH , Smith JL , Skiniotis G
Ref : Nature , 510 :560 , 2014
Abstract : The polyketide synthase (PKS) mega-enzyme assembly line uses a modular architecture to synthesize diverse and bioactive natural products that often constitute the core structures or complete chemical entities for many clinically approved therapeutic agents. The architecture of a full-length PKS module from the pikromycin pathway of Streptomyces venezuelae creates a reaction chamber for the intramodule acyl carrier protein (ACP) domain that carries building blocks and intermediates between acyltransferase, ketosynthase and ketoreductase active sites (see accompanying paper). Here we determine electron cryo-microscopy structures of a full-length pikromycin PKS module in three key biochemical states of its catalytic cycle. Each biochemical state was confirmed by bottom-up liquid chromatography/Fourier transform ion cyclotron resonance mass spectrometry. The ACP domain is differentially and precisely positioned after polyketide chain substrate loading on the active site of the ketosynthase, after extension to the beta-keto intermediate, and after beta-hydroxy product generation. The structures reveal the ACP dynamics for sequential interactions with catalytic domains within the reaction chamber, and for transferring the elongated and processed polyketide substrate to the next module in the PKS pathway. During the enzymatic cycle the ketoreductase domain undergoes dramatic conformational rearrangements that enable optimal positioning for reductive processing of the ACP-bound polyketide chain elongation intermediate. These findings have crucial implications for the design of functional PKS modules, and for the engineering of pathways to generate pharmacologically relevant molecules.
ESTHER : Whicher_2014_Nature_510_560
PubMedSearch : Whicher_2014_Nature_510_560
PubMedID: 24965656

Title : The first total synthesis of (+\/-)-cyclophostin and (+\/-)-cyclipostin P: inhibitors of the serine hydrolases acetyl cholinesterase and hormone sensitive lipase - Malla_2011_Org.Lett_13_3094
Author(s) : Malla RK , Bandyopadhyay S , Spilling CD , Dutta S , Dupureur CM
Ref : Org Lett , 13 :3094 , 2011
Abstract : Cyclophostin, a structurally unique and potent naturally occurring acetyl cholinesterase (AChE) inhibitor, and its unnatural diastereomer were prepared in 6 steps and 15% overall yield from hydroxymethyl butyrolactone. The unnatural diastereomer of cyclophostin was converted into cyclipostin P, a potent naturally occurring hormone sensitive lipase (HSL) inhibitor, using a one pot dealkylation-alkylation process. The inhibition [IC(50)] of human AChE by cyclophostin and its diastereomer are reported, as well as constituent binding (K(I)) and reactivity (k(2)) constants.
ESTHER : Malla_2011_Org.Lett_13_3094
PubMedSearch : Malla_2011_Org.Lett_13_3094
PubMedID: 21591624

Title : Synthesis and kinetic analysis of some phosphonate analogs of cyclophostin as inhibitors of human acetylcholinesterase - Dutta_2010_Bioorg.Med.Chem_18_2265
Author(s) : Dutta S , Malla RK , Bandyopadhyay S , Spilling CD , Dupureur CM
Ref : Bioorganic & Medicinal Chemistry , 18 :2265 , 2010
Abstract : Two new monocyclic analogs of the natural AChE inhibitor cyclophostin and two exocyclic enol phosphates were synthesized. The potencies and mechanisms of inhibition of the bicyclic and monocyclic enol phosphonates and the exocyclic enol phosphates toward human AChE are examined. One diastereoisomer of the bicyclic phosphonate exhibits an IC(50) of 3 microM. Potency is only preserved when the cyclic enol phosphonate is intact and conjugated to an ester. Kinetic analysis indicates both a binding and a slow inactivation step for all active compounds. Mass spectrometric analysis indicates that the active site Ser is indeed phosphorylated by the bicyclic phosphonate.
ESTHER : Dutta_2010_Bioorg.Med.Chem_18_2265
PubMedSearch : Dutta_2010_Bioorg.Med.Chem_18_2265
PubMedID: 20189400

Title : Production and characterization of an alkaline thermostable crude lipase from an isolated strain of Bacillus cereus C(7) - Dutta_2009_Appl.Biochem.Biotechnol_159_142
Author(s) : Dutta S , Ray L
Ref : Appl Biochem Biotechnol , 159 :142 , 2009
Abstract : A bacterial strain isolated from spoiled coconut and identified as Bacillus cereus was found capable of producing alkaline thermostable extracellular lipase. Optimum temperature, time, and pH for enzyme substrate reaction were found to be 60 degrees C, 10 min, and 8.0 respectively. Common surfactants except Triton X 100 and cetyltrimethylammonium bromide have no or very little inhibitory effects on enzyme activity. The enzyme was found to be stable in presence of oxidizing agents and protease enzyme. The maximum lipase production was achieved at 30-33 degrees C, pH 8.0 on 24 h of fermentation using 50 ml medium in a 250-ml Erlenmeyer flask. The superior carbon and nitrogen sources for lipase production were starch (2%) and ammonium sulfate (nitrogen level 21.2 mg/100 ml), peptone (nitrogen level 297 mg/100 ml), and urea (nitrogen level 46.62 mg/100 ml) in combination, respectively. The maximum enzyme activity obtained was 33 +/- 0.567 IU/ml.
ESTHER : Dutta_2009_Appl.Biochem.Biotechnol_159_142
PubMedSearch : Dutta_2009_Appl.Biochem.Biotechnol_159_142
PubMedID: 19198766

Title : Synthesis and biological evaluation of a phosphonate analog of the natural acetyl cholinesterase inhibitor cyclophostin - Bandyopadhyay_2008_J.Org.Chem_73_8386
Author(s) : Bandyopadhyay S , Dutta S , Spilling CD , Dupureur CM , Rath NP
Ref : J Org Chem , 73 :8386 , 2008
Abstract : Two diastereomers of a phosphonate analog 6 of the AChE inhibitor cyclophostin were synthesized. The substitution reaction of phosphono allylic carbonate 10a with methyl acetoacetate gave the vinyl phosphonate 9a. Attempted hydrogenation/debenzylation gave an unexpected enolether lactone. Alternatively, selective hydrogenation, demethylation, cyclization and debenzylation gave the phosphonate analog of cyclophostin as a separable mixture of diastereomers 6. The trans phosphonate isomer was more active than the cis isomer against AChE from two sources.
ESTHER : Bandyopadhyay_2008_J.Org.Chem_73_8386
PubMedSearch : Bandyopadhyay_2008_J.Org.Chem_73_8386
PubMedID: 18821801