X-ray crystal structure determination of petrosterol p-bromobenzoate. A revision

Mattia, Carlo Andrea; Mazzarella, L.; Puliti, R.; Sica, Donato; Zollo, Franco

doi:10.1016/s0040-4039(01)95108-1

Cited by 38 publications

(14 citation statements)

References 3 publications

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“…The 1 H and 13 C chemical shifts at the C-3/28 positions of 1-3 were very similar to each other. The significant difference in the chemical shifts between 1 and 2 was detected on the signals due to the C-14/17 positions (Table 1).…”

Section: Structure Elucidationsupporting

confidence: 58%

“…Compounds 2-5 were identified as petrosynol (2), 9,10) adociacetylene D (3), 11,12) (5R)-3,15,27-triacontatriene-1,29-diyn-5-ol (4), 12) and petrosterol (5), 13,14) respectively, by comparing their spectroscopic data with those in the literature.…”

Section: Resultsmentioning

confidence: 99%

“…panicea collected at Iriomote Island exhibited inhibitory activity against PTP1B. Bioassay-guided separation led to the isolation of a new polyacetylene, named isopetrosynol (1), together with four known compounds [9][10][11][12][13][14] : petrosynol (2), adociacetylene D (3), (5R)-3,15,27-triacontatriene-1,29-diyn-5-ol (4), and petrosterol (5) (Fig. 1).…”

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confidence: 99%

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Isopetrosynol, a New Protein Tyrosine Phosphatase 1B Inhibitor, from the Marine Sponge Halichondria cf. panicea Collected at Iriomote Island

Abdjul

Yamazaki

Takahashi

et al. 2016

CHEMICAL & PHARMACEUTICAL BULLETIN

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A new polyacetylene compound, isopetrosynol (1), was isolated from the Okinawan marine sponge Halichondria cf. panicea together with petrosynol (2), adociacetylene D (3), (5R)-3,15,27-triacontatriene-1,29-diyn-5-ol (4), and petrosterol (5). The structure of 1 was assigned on the basis of spectroscopic data for 1 and 2. Compound 1 inhibited protein tyrosine phosphatase 1B (PTP1B) activity with an IC50 value of 8.2±0.3 µM, while compound 2, a diastereomer of 1, showed only 28.9±4.5% inhibition at 21.6 µM. The IC50 values of compounds 3 and 4 were 7.8±0.5 and 12.2±0.5 µM, respectively. Oleanolic acid, a positive control, inhibited PTP1B activity at 0.7±0.1 µM (IC50) in the same experiment. The inhibitory activity of 1 was stronger than that of its diastereomer (2). This is the first study to show the inhibitory effects of polyacetylene compounds on PTP1B.

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Section: Structure Elucidationsupporting

confidence: 58%

Section: Resultsmentioning

confidence: 99%

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Isopetrosynol, a New Protein Tyrosine Phosphatase 1B Inhibitor, from the Marine Sponge Halichondria cf. panicea Collected at Iriomote Island

Abdjul

Yamazaki

Takahashi

et al. 2016

CHEMICAL & PHARMACEUTICAL BULLETIN

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“…Previously, various studies on the chemical constituents of Petrosia sp. led to the isolation of cyclosterols [4,5,6], polyacetylenic alcohols [7,8,9,10,11,12], meroditerpenes [13,14,15], 1,2-dihydroisoquinolines [16], halenaquinones [17], and pyridoacridine alkaloids [18]. Among them, some exhibited significant biological effects such as cytotoxicity [9,10,12,19,20,21], neurotrophic [11], antifouling [22] and antimicrobial activities [21], inhibitions against proteasome [15], protein Tyrosine phosphate 1B [13], cholinesterase [18], as well as inhibitory effects of the receptor activator of nuclear factor κB ligand (RANKL) induced osteoclastogenesis [17].…”

Section: Introductionmentioning

confidence: 99%

Sterols from Thai Marine Sponge Petrosia (Strongylophora) sp. and Their Cytotoxicity

et al. 2017

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“…2) Cyclopropanedicarboxylates have been studied only rarely inspite of the fact that cyclopropane derivatives have become versatile building blocks for the synthesis of various natural products [20-223.3) Cyclopropane rings also occur as structural elements of natural products, e.g. cyclopropaneamino acids [23] [24], cyclopropane fatty acids [25], and steroids [26] [27]. Many mono-and sesquiterpenes contain a cyclopropane ring [25].…”

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confidence: 99%

Stereoselective Hydrolysis of Substituted Cyclopropanedicarboxylates with Pig Liver Esterase

Walser¹,

Renold²,

N'Goka³

et al. 1991

Helvetica Chimica Acta

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The hydrolysis of the rneso-cyclopropane-l,2-dicarboxylates la-3a, 4, 5a, 6a, and 9, containing various substituents at C(3), and of the rac-3-phenylcyclopropane-1,2-dicarboxylates 7a, Sa, and 10 with pig liver esterase (PLE) is described. The stereoselectivity and absolute configurations of the products were determined. An interpretation of results was attempted on the basis of a recent active-site model for PLE.Introduction. -The efficient synthesis of biologically active compounds, either of natural or unnatural origin, frequently requires chiral synthons. Enzymes as chiral catalysts are now widely used for their preparation [l-41, because it often is rather difficult to introduce centres or chirality or perform regiospecific transformations by the application of purely 'chemical methods'. Especially esterases, such as pig liver esterase (PLE, E.C. 3.1.1.1), a serine hydrolase, have been studied extensively in recent years [5-81. We have used PLE successfully in resolving racemic esters [9] and for the preparation of versatile chirons [5] [6] [9] [lo]. Stability, low costs, and the ability of hydrolyse a wide range of substrates with high stereoselectivity represent additional advantages of this enzyme which operates-without the need for co-enzymes. Until now, more than one hundred different esters, mainly meso-and prochiral-diesters have been subjected to the treatment with PLE [8]. To be able to fully exploit the potential of this enzyme, it is indispensable to understand the factors which are responsible for the specificity. Accordingly, we as well as other research groups have initiated investigations for securing a large number of data on hydrolyses, allowing to gain more insight into the relationship between substrate structure and enzymic activity of PLE. Until recently, it appeared to be very difficult to reach this goal, not only because the physiological role of PLE is unknown [ 1 I], but also because commercially available PLE preparations are mixtures of at least six isoenzymes [12] [ 131 which, however, were found to exhibit essentially the same stereospecificity [14]. These findings justify the attempt to rationalize the results of the hydrolyses by an active-site model which is mainly based on the measured ee values and the absolute configuration of the hydrolysis products. Several approaches to such a model have been reported [14-181. The most recent proposal made by Jones and coworkers which is based on cubic-space descriptors, is at present the most precise published active-site model [19].Here, we report on the results of the hydrolysis of a series of structurally related cyclopropane-l,2-~arboxylates with PLE. These substrates were chosen for the following reasons: I ) The cyclopropane ring provides rigidity. Therefore, only one preferred conformation has to be accounted for the analysis of the substrate/active-site interac-

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X-ray crystal structure determination of petrosterol p-bromobenzoate. A revision

Cited by 38 publications

References 3 publications

Isopetrosynol, a New Protein Tyrosine Phosphatase 1B Inhibitor, from the Marine Sponge <i>Halichondria</i> cf. <i>panicea</i> Collected at Iriomote Island

Isopetrosynol, a New Protein Tyrosine Phosphatase 1B Inhibitor, from the Marine Sponge <i>Halichondria</i> cf. <i>panicea</i> Collected at Iriomote Island

Sterols from Thai Marine Sponge Petrosia (Strongylophora) sp. and Their Cytotoxicity

Stereoselective Hydrolysis of Substituted Cyclopropanedicarboxylates with Pig Liver Esterase

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