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Christopher R. Parish - One of the best experts on this subject based on the ideXlab platform.
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use of sulfated linked Cyclitols as heparan sulfate mimetics to probe the heparin heparan sulfate binding specificity of proteins
Journal of Biological Chemistry, 2005Co-Authors: Craig Freeman, Vito Ferro, Martin G. Banwell, Ligong Liu, Kathryn J. Brown, Anna Bezos, Christopher R. ParishAbstract:Heparin and heparan sulfate (HS) are structurally diverse glycosaminoglycans (GAG) that are known to interact, via unique structural motifs, with a wide range of functionally distinct proteins and modulate their biological activity. To define the GAG motifs that interact with proteins, we assessed the ability of 15 totally synthetic HS mimetics to interact with 10 functionally diverse proteins that bind heparin/HS. The HS mimetics consisted of Cyclitol-based pseudo-sugars coupled by linkers of variable chain length, flexibility, orientation, and hydrophobicity, with variations in sulfation also being introduced into some molecules. Three of the proteins tested, namely hepatocyte growth factor, eotaxin, and elastase, failed to interact with any of the sulfated linked Cyclitols. In contrast, each of the remaining seven proteins tested exhibited a unique reactivity pattern with the panel of HS mimetics, with tetrameric Cyclitols linked by different length alkyl chains being particularly informative. Thus, compounds with short alkyl spacers (2–3 carbon atoms) effectively blocked the interaction of fibroblast growth factor-1 (FGF-1) and lipoprotein lipase with heparin/HS, whereas longer chain spacers (7–10 carbon atoms) were required for optimal inhibition of FGF-2 and vascular endothelial growth factor binding. This effect was most pronounced with the chemokine, interleukin-8, where alkyl-linked tetrameric Cyclitols were essentially inactive unless a spacer of >7 carbon atoms was used. The heparin-inhibitable enzymes heparanase and cathepsin G also displayed characteristic inhibition patterns, cathepsin G interacting promiscuously with most of the sulfated Cyclitols but heparanase activity being inhibited most effectively by HS mimetics that structurally resemble a sulfated pentasaccharide. These data indicate that a simple panel of HS mimetics can be used to probe the HS binding specificity of proteins, with the position of anionic groups in the HS mimetics being critical.
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Use of Sulfated Linked Cyclitols as Heparan Sulfate Mimetics to Probe the Heparin/Heparan Sulfate Binding Specificity of Proteins
The Journal of biological chemistry, 2005Co-Authors: Craig Freeman, Vito Ferro, Martin G. Banwell, Ligong Liu, Kathryn J. Brown, Anna Bezos, Christopher R. ParishAbstract:Heparin and heparan sulfate (HS) are structurally diverse glycosaminoglycans (GAG) that are known to interact, via unique structural motifs, with a wide range of functionally distinct proteins and modulate their biological activity. To define the GAG motifs that interact with proteins, we assessed the ability of 15 totally synthetic HS mimetics to interact with 10 functionally diverse proteins that bind heparin/HS. The HS mimetics consisted of Cyclitol-based pseudo-sugars coupled by linkers of variable chain length, flexibility, orientation, and hydrophobicity, with variations in sulfation also being introduced into some molecules. Three of the proteins tested, namely hepatocyte growth factor, eotaxin, and elastase, failed to interact with any of the sulfated linked Cyclitols. In contrast, each of the remaining seven proteins tested exhibited a unique reactivity pattern with the panel of HS mimetics, with tetrameric Cyclitols linked by different length alkyl chains being particularly informative. Thus, compounds with short alkyl spacers (2–3 carbon atoms) effectively blocked the interaction of fibroblast growth factor-1 (FGF-1) and lipoprotein lipase with heparin/HS, whereas longer chain spacers (7–10 carbon atoms) were required for optimal inhibition of FGF-2 and vascular endothelial growth factor binding. This effect was most pronounced with the chemokine, interleukin-8, where alkyl-linked tetrameric Cyclitols were essentially inactive unless a spacer of >7 carbon atoms was used. The heparin-inhibitable enzymes heparanase and cathepsin G also displayed characteristic inhibition patterns, cathepsin G interacting promiscuously with most of the sulfated Cyclitols but heparanase activity being inhibited most effectively by HS mimetics that structurally resemble a sulfated pentasaccharide. These data indicate that a simple panel of HS mimetics can be used to probe the HS binding specificity of proteins, with the position of anionic groups in the HS mimetics being critical.
Wolfgang Piepersberg - One of the best experts on this subject based on the ideXlab platform.
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biosynthesis of the c 7 Cyclitol moiety of acarbose in actinoplanes species se50 110 7 o phosphorylation of the initial Cyclitol precursor leads to proposal of a new biosynthetic pathway
Journal of Biological Chemistry, 2002Co-Authors: Changsheng Zhang, Ansgar Stratmann, Oliver Block, Ralph Bruckner, Michael Podeschwa, Hansjosef Altenbach, Udo F Wehmeier, Michael Podeschwa, Wolfgang PiepersbergAbstract:Abstract We have previously demonstrated that the biosynthesis of the C7-Cyclitol, called valienol (or valienamine), of the α-glucosidase inhibitor acarbose starts from the cyclization of sedo-heptulose 7-phosphate to 2-epi-5-epi-valiolone (Stratmann, A., Mahmud, T., Lee, S., Distler, J., Floss, H. G., and Piepersberg, W. (1999)J. Biol. Chem. 274, 10889–10896). Synthesis of the intermediate 2-epi-5-epi-valiolone is catalyzed by the cyclase AcbC encoded in the biosynthetic (acb) gene cluster of Actinoplanes sp. SE50/110. The acbCgene lies in a possible transcription unit, acbKLMNOC, cluster encompassing putative biosynthetic genes for Cyclitol conversion. All genes were heterologously expressed in strains ofStreptomyces lividans 66 strains 1326, TK23, and TK64. The AcbK protein was identified as the acarbose 7-kinase, which had been described earlier (Drepper, A., and Pape, H. (1996) J. Antibiot. (Tokyo) 49, 664–668). The multistep conversion of 2-epi-5-epi-valiolone to the final Cyclitol moiety was studied by testing enzymatic mechanisms such as dehydration, reduction, epimerization, and phosphorylation. Thus, a phosphotransferase activity was identified modifying 2-epi-5-epi-valiolone by ATP-dependent phosphorylation. This activity could be attributed to the AcbM protein by verifying this activity inS. lividans strain TK64/pCW4123M, expressing His-tagged AcbM. The His-tagged AcbM protein was purified and subsequently characterized as a 2-epi-5-epi-valiolone 7-kinase, presumably catalyzing the first enzyme reaction in the biosynthetic route, leading to an activated form of the intermediate 1-epi-valienol. The AcbK protein could not catalyze the same reaction nor convert any of the other C7-Cyclitol monomers tested. The 2-epi-5-epi-valiolone 7-phosphate was further converted by the AcbO protein to another isomeric and phosphorylated intermediate, which was likely to be the 2-epimer 5-epi-valiolone 7-phosphate. The products of both enzyme reactions were characterized by mass spectrometric methods. The product of the AcbM-catalyzed reaction, 2-epi-5-epi-valiolone 7-phosphate, was purified on a preparative scale and identified by NMR spectroscopy. A biosynthetic pathway for the pseudodisaccharidic acarviosyl moiety of acarbose is proposed on the basis of these data.
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Biosynthesis of the C(7)-Cyclitol moiety of acarbose in Actinoplanes species SE50/110. 7-O-phosphorylation of the initial Cyclitol precursor leads to proposal of a new biosynthetic pathway.
The Journal of biological chemistry, 2002Co-Authors: Changsheng Zhang, Ansgar Stratmann, Oliver Block, Ralph Bruckner, Michael Podeschwa, Hansjosef Altenbach, Udo F Wehmeier, Wolfgang PiepersbergAbstract:Abstract We have previously demonstrated that the biosynthesis of the C7-Cyclitol, called valienol (or valienamine), of the α-glucosidase inhibitor acarbose starts from the cyclization of sedo-heptulose 7-phosphate to 2-epi-5-epi-valiolone (Stratmann, A., Mahmud, T., Lee, S., Distler, J., Floss, H. G., and Piepersberg, W. (1999)J. Biol. Chem. 274, 10889–10896). Synthesis of the intermediate 2-epi-5-epi-valiolone is catalyzed by the cyclase AcbC encoded in the biosynthetic (acb) gene cluster of Actinoplanes sp. SE50/110. The acbCgene lies in a possible transcription unit, acbKLMNOC, cluster encompassing putative biosynthetic genes for Cyclitol conversion. All genes were heterologously expressed in strains ofStreptomyces lividans 66 strains 1326, TK23, and TK64. The AcbK protein was identified as the acarbose 7-kinase, which had been described earlier (Drepper, A., and Pape, H. (1996) J. Antibiot. (Tokyo) 49, 664–668). The multistep conversion of 2-epi-5-epi-valiolone to the final Cyclitol moiety was studied by testing enzymatic mechanisms such as dehydration, reduction, epimerization, and phosphorylation. Thus, a phosphotransferase activity was identified modifying 2-epi-5-epi-valiolone by ATP-dependent phosphorylation. This activity could be attributed to the AcbM protein by verifying this activity inS. lividans strain TK64/pCW4123M, expressing His-tagged AcbM. The His-tagged AcbM protein was purified and subsequently characterized as a 2-epi-5-epi-valiolone 7-kinase, presumably catalyzing the first enzyme reaction in the biosynthetic route, leading to an activated form of the intermediate 1-epi-valienol. The AcbK protein could not catalyze the same reaction nor convert any of the other C7-Cyclitol monomers tested. The 2-epi-5-epi-valiolone 7-phosphate was further converted by the AcbO protein to another isomeric and phosphorylated intermediate, which was likely to be the 2-epimer 5-epi-valiolone 7-phosphate. The products of both enzyme reactions were characterized by mass spectrometric methods. The product of the AcbM-catalyzed reaction, 2-epi-5-epi-valiolone 7-phosphate, was purified on a preparative scale and identified by NMR spectroscopy. A biosynthetic pathway for the pseudodisaccharidic acarviosyl moiety of acarbose is proposed on the basis of these data.
Marianne Popp - One of the best experts on this subject based on the ideXlab platform.
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Cyclitols protect glutamine synthetase and malate dehydrogenase against heat induced deactivation and thermal denaturation
Biochemical and Biophysical Research Communications, 2006Co-Authors: Martina Jaindl, Marianne PoppAbstract:The accumulation of Cyclitols in plants is a widespread response that provides protection against various environmental stresses. The capacity of myo-Inositol, pinitol, quercitol, and other compatible solutes (i.e., sorbitol, proline, and glycinebetaine) to protect proteins against thermally induced denaturation and deactivation was examined. Enzymatic activity measurements of L-glutamine synthetase from Escherichia coli and Hordeum vulgare showed that the presence of Cyclitols during heat treatment resulted in a significantly higher percentage of residual activity. CD spectroscopy experiments were used to study thermal stabilities of protein secondary structures upon the addition of myo-Inositol, pinitol, and glucose. 0.4 M myo-Inositol was observed to raise the melting temperature (Tm) of GS from E. coli by 3.9 degrees C and MDH from pig heart by 3.4 degrees C, respectively. Pinitol showed an increase in Tm of MDH by 3.8 degrees C, whereas glucose was not effective. Our results show a great potential of stabilizing proteins by the addition of Cyclitols.
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Cyclitols protect glutamine synthetase and malate dehydrogenase against heat induced deactivation and thermal denaturation.
Biochemical and biophysical research communications, 2006Co-Authors: Martina Jaindl, Marianne PoppAbstract:Abstract The accumulation of Cyclitols in plants is a widespread response that provides protection against various environmental stresses. The capacity of myo -Inositol, pinitol, quercitol, and other compatible solutes (i.e., sorbitol, proline, and glycinebetaine) to protect proteins against thermally induced denaturation and deactivation was examined. Enzymatic activity measurements of l -glutamine synthetase from Escherichia coli and Hordeum vulgare showed that the presence of Cyclitols during heat treatment resulted in a significantly higher percentage of residual activity. CD spectroscopy experiments were used to study thermal stabilities of protein secondary structures upon the addition of myo -Inositol, pinitol, and glucose. 0.4 M myo -Inositol was observed to raise the melting temperature ( T m ) of GS from E. coli by 3.9 °C and MDH from pig heart by 3.4 °C, respectively. Pinitol showed an increase in T m of MDH by 3.8 °C, whereas glucose was not effective. Our results show a great potential of stabilizing proteins by the addition of Cyclitols.
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Cyclitols as cryoprotectants for spinach and chickpea thylakoids
Environmental and experimental botany, 2000Co-Authors: Birgit Orthen, Marianne PoppAbstract:Abstract Thylakoid membranes isolated from either spinach or chickpea leaves were used as a model system for evaluating the capacity of Cyclitols to act as cryoprotectants. The effect of freezing for 3 h at −18°C on cyclic photophosphorylation and electron transport was measured. The Cyclitols, ononitol, O -methyl- muco -inositol, pinitol, quebrachitol and quercitol at 50–150 mol m −3 decreased membrane damage by freezing and thawing to a similar degree as the well known cryoprotectants sucrose and trehalose. On addition of the cryotoxic solute NaCl (100 mol m −3 ) to the test system these methylated cyclohexanhexols again provided a protection comparable to that of the two disaccharides. Quercitol (cyclohexanpentol) was not effective when added in lower concentrations (50–100 mol m −3 ) and in case of this Cyclitol a ratio of membrane toxic to membrane compatible solute of 0.66 was apparently needed to prevent a loss of cyclic photophosphorylation. Little difference was observed in the results from spinach or chickpea thylakoids although these plants naturally accumulate different cyto-solutes (spinach: glycinebetaine; chickpea: pinitol).
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Hydroxyl radical scavenging properties of Cyclitols
Proceedings of the Royal Society of Edinburgh. Section B. Biological Sciences, 1994Co-Authors: Birgit Orthen, Marianne Popp, Nicholas SmirnoffAbstract:Cyclitols are low molecular weight substances which accumulate in plant cells in response to various environmental stress situations, for example drought (Ford 1984), salinity (Gorham et al . 1984), low temperature (Richter et al . 1990). Apart from their more general role in osmotic adjustment, only in the case of salt stress is their mode of function well understood. Cyclitols (e.g. pinitol) accumulate when plants are exposed to increasing salt concentration (Paul & Cockburn 1989) and act as compatible solutes (Sommer et al . 1990) as defined by Brown & Simpson (1972). The significance of Cyclitol accumulation in stress adaptation of plants to drought and cold still remains uncertain. However, it is generally accepted that drought and cold as well as several other stress situations lead to an enhanced generation of oxygen free radicals (Elstner 1990; Smirnoff & Colombe 1988), including the hydroxyl radical as the most harmful one. The report by Smirnoff & Cumbes (1989) that myo-inositol is an effective hydroxyl radical scavenger prompted us to test other naturally-occuring Cyclitols like pinitol, quebrachitol, 1-D-1-O-methyl-muco-inositol, ononitol and quercitol for their ability to scavenge hydroxyl radicals.
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The physiological importance of accumulation of Cyclitols in Viscum album L.
New Phytologist, 1992Co-Authors: Andreas Richter, Marianne PoppAbstract:SUMMARY Investigations of Viscum album on 16 different host species revealed an endogenous Cyclitol pattern with pinitol, 1-O-methyl-muco-inositol, quebrachitol, chiro-inositol, an unidentified O-methyl-inositol and traces of ononitol. Host-specific Cyclitols including bornesitol, quercitol, viburnitol, scyllo-inositol and the hexitol, sorbitol, were also stored in the mistletoe. The endogenous Cyclitols were accumulated to such high concentrations that they made a large contribution to the osmotic potential. It was estimated that 22.6–43 % of mistletoe carbon is derived from the host.
Craig Freeman - One of the best experts on this subject based on the ideXlab platform.
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use of sulfated linked Cyclitols as heparan sulfate mimetics to probe the heparin heparan sulfate binding specificity of proteins
Journal of Biological Chemistry, 2005Co-Authors: Craig Freeman, Vito Ferro, Martin G. Banwell, Ligong Liu, Kathryn J. Brown, Anna Bezos, Christopher R. ParishAbstract:Heparin and heparan sulfate (HS) are structurally diverse glycosaminoglycans (GAG) that are known to interact, via unique structural motifs, with a wide range of functionally distinct proteins and modulate their biological activity. To define the GAG motifs that interact with proteins, we assessed the ability of 15 totally synthetic HS mimetics to interact with 10 functionally diverse proteins that bind heparin/HS. The HS mimetics consisted of Cyclitol-based pseudo-sugars coupled by linkers of variable chain length, flexibility, orientation, and hydrophobicity, with variations in sulfation also being introduced into some molecules. Three of the proteins tested, namely hepatocyte growth factor, eotaxin, and elastase, failed to interact with any of the sulfated linked Cyclitols. In contrast, each of the remaining seven proteins tested exhibited a unique reactivity pattern with the panel of HS mimetics, with tetrameric Cyclitols linked by different length alkyl chains being particularly informative. Thus, compounds with short alkyl spacers (2–3 carbon atoms) effectively blocked the interaction of fibroblast growth factor-1 (FGF-1) and lipoprotein lipase with heparin/HS, whereas longer chain spacers (7–10 carbon atoms) were required for optimal inhibition of FGF-2 and vascular endothelial growth factor binding. This effect was most pronounced with the chemokine, interleukin-8, where alkyl-linked tetrameric Cyclitols were essentially inactive unless a spacer of >7 carbon atoms was used. The heparin-inhibitable enzymes heparanase and cathepsin G also displayed characteristic inhibition patterns, cathepsin G interacting promiscuously with most of the sulfated Cyclitols but heparanase activity being inhibited most effectively by HS mimetics that structurally resemble a sulfated pentasaccharide. These data indicate that a simple panel of HS mimetics can be used to probe the HS binding specificity of proteins, with the position of anionic groups in the HS mimetics being critical.
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Use of Sulfated Linked Cyclitols as Heparan Sulfate Mimetics to Probe the Heparin/Heparan Sulfate Binding Specificity of Proteins
The Journal of biological chemistry, 2005Co-Authors: Craig Freeman, Vito Ferro, Martin G. Banwell, Ligong Liu, Kathryn J. Brown, Anna Bezos, Christopher R. ParishAbstract:Heparin and heparan sulfate (HS) are structurally diverse glycosaminoglycans (GAG) that are known to interact, via unique structural motifs, with a wide range of functionally distinct proteins and modulate their biological activity. To define the GAG motifs that interact with proteins, we assessed the ability of 15 totally synthetic HS mimetics to interact with 10 functionally diverse proteins that bind heparin/HS. The HS mimetics consisted of Cyclitol-based pseudo-sugars coupled by linkers of variable chain length, flexibility, orientation, and hydrophobicity, with variations in sulfation also being introduced into some molecules. Three of the proteins tested, namely hepatocyte growth factor, eotaxin, and elastase, failed to interact with any of the sulfated linked Cyclitols. In contrast, each of the remaining seven proteins tested exhibited a unique reactivity pattern with the panel of HS mimetics, with tetrameric Cyclitols linked by different length alkyl chains being particularly informative. Thus, compounds with short alkyl spacers (2–3 carbon atoms) effectively blocked the interaction of fibroblast growth factor-1 (FGF-1) and lipoprotein lipase with heparin/HS, whereas longer chain spacers (7–10 carbon atoms) were required for optimal inhibition of FGF-2 and vascular endothelial growth factor binding. This effect was most pronounced with the chemokine, interleukin-8, where alkyl-linked tetrameric Cyclitols were essentially inactive unless a spacer of >7 carbon atoms was used. The heparin-inhibitable enzymes heparanase and cathepsin G also displayed characteristic inhibition patterns, cathepsin G interacting promiscuously with most of the sulfated Cyclitols but heparanase activity being inhibited most effectively by HS mimetics that structurally resemble a sulfated pentasaccharide. These data indicate that a simple panel of HS mimetics can be used to probe the HS binding specificity of proteins, with the position of anionic groups in the HS mimetics being critical.
Bogusław Buszewski - One of the best experts on this subject based on the ideXlab platform.
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Effects of growth conditions and cultivability on the content of Cyclitols in Medicago sativa
International Journal of Environmental Science and Technology, 2020Co-Authors: F. Monedeiro, Hossam Al-suod, Magdalena Ligor, Ileana-andreea Rațiu, Bogusław BuszewskiAbstract:Cyclitols are secondary metabolites with bioactive properties, naturally occurring in plants. Accumulation of such metabolites is directly connected with abiotic stressing factors. This article investigates the influence exercised by a series of abiotic factors including plant treatment with elicitors and cultivability in various regions of Europe, in some cases during two seasons, onto the amounts of Cyclitols produced in alfalfa ( Medicago sativa L.). The obtained results highlighted that NaCl elicitation acts to increase the quantity of Cyclitols, while AgNO_3 and Zn(NO_3)_2 generally decreased the obtained amount of Cyclitols. When considering the seasonal impact, samples harvested in August presented a double amount of Cyclitols in comparison with those collected in May. Correlation analysis proved that this phenomenon is related mainly to sunshine period versus low humidity. However, our investigation suggests that soil type, salinity level, lack of humidity, the number of sunny days, and plant elicitation play a role on the amount of Cyclitols produced in alfalfa plant.
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Effects of growth conditions and cultivability on the content of Cyclitols in Medicago sativa
International Journal of Environmental Science and Technology, 2020Co-Authors: Ileana-andreea Rațiu, Hossam Al-suod, Magdalena Ligor, F. Monedeiro, Bogusław BuszewskiAbstract:Cyclitols are secondary metabolites with bioactive properties, naturally occurring in plants. Accumulation of such metabolites is directly connected with abiotic stressing factors. This article investigates the influence exercised by a series of abiotic factors including plant treatment with elicitors and cultivability in various regions of Europe, in some cases during two seasons, onto the amounts of Cyclitols produced in alfalfa ( Medicago sativa L.). The obtained results highlighted that NaCl elicitation acts to increase the quantity of Cyclitols, while AgNO_3 and Zn(NO_3)_2 generally decreased the obtained amount of Cyclitols. When considering the seasonal impact, samples harvested in August presented a double amount of Cyclitols in comparison with those collected in May. Correlation analysis proved that this phenomenon is related mainly to sunshine period versus low humidity. However, our investigation suggests that soil type, salinity level, lack of humidity, the number of sunny days, and plant elicitation play a role on the amount of Cyclitols produced in alfalfa plant.
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Simultaneous Determination of Cyclitols and Sugars Following a Comprehensive Investigation of 40 Plants
Food Analytical Methods, 2019Co-Authors: Tomasz Ligor, Hossam Al-suod, Magdalena Ligor, Ileana-andreea Rațiu, Aneta Krakowska, Ryszard Górecki, Bogusław BuszewskiAbstract:Due to the important features of widely unexplored Cyclitols, a comprehensive qualitative and quantitative study is needed. Moreover, measuring the possible available amounts of identified components in plant material represents a stringent need, due to their importance in phytomedicine and their use in food. The purpose of this study was to realize an extended investigation mainly of Cyclitols, but of sugars and sugar alcohols as well, from natural sources. Thus, 17 target compounds (7 Cyclitols and 2 sugar alcohols and 8 sugars) extracted from medicinal and edible plants are reported. All detected components were simultaneous separated in just one chromatographic run, using a single GC column. A number of 52 sources coming from 40 species were studied. Thus, we report 37 new sources of Cyclitols. Moreover, almost for all Cyclitols, the richest source was not investigated previously. Therefore, the obtained results can represent a valuable material for food, pharmaceutical, medical, or cosmetic industry interested in the use of Cyclitols.
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Pressurized liquid extraction of Cyclitols and sugars: optimization of extraction parameters and selective separation.
Journal of separation science, 2019Co-Authors: Hossam Al-suod, Ryszard J. Górecki, Ileana-andreea Rațiu, Bogusław BuszewskiAbstract:Cyclitols and sugars were obtained as a mixture from Medicago sativa L., in a comparative study by using maceration, and pressurized liquid extraction, as a modern and green extraction techniques. The influence of extraction parameters including: extraction temperature, time and number of cycles on the content of sugars and Cyclitols was investigated based on response surface methodology. The highest total amount of sugars and Cyclitols (62.27 ± 2.30 and 50.35 ± 0.77 mg/g of dry material, respectively) was obtained when extraction was performed at 88°C, for 22 min, in two cycles. The methodology used involved extraction, purification, selective separation (using yeast and anion exchange resin) and derivatization, followed by gas chromatography -mass spectrometry analysis. The use of yeast treatment realized an effective fractionation of Cyclitols and sugars, which allowed the removal of most sugars. The involvement of anion exchange resin after yeast allowed the removal of sugar alcohols and lactose, together with other sugar traces remained and to obtain a solution containing six Cyclitols. The recrystallization of dry residue after solvent evaporation, from ethanol, allowed us to obtain 14.65 mg of white pure crystals identified with NMR spectroscopy, liquid chromatography with mass spectrometry, gas chromatography with mass spectrometry, optical rotation and melting point as analysis D-pinitol.
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The Healing-Promoting Properties of Selected Cyclitols—A Review
Nutrients, 2018Co-Authors: Agnieszka Owczarczyk-saczonek, Lesław B. Lahuta, Ryszard J. Górecki, Magdalena Ligor, Waldemar Placek, Bogusław BuszewskiAbstract:Introduction: Myo-inositol and its derivatives Cyclitols play an important role in the processes of cell regulation, signal transduction, osmoregulation, and ion channel physiology, and are a component of the cell membrane. Free Cyclitols present in food or released during the degradation of galactosyl Cyclitols by bacteria (in digestive tract) show some physiological benefits. Aim: The aim of this paper is to present and analyze the documented data about curative and healing properties of Cyclitols. Results and discussion: Cyclitols are well known compounds in the treatment of an accompanied diabetes insulin resistance, and also obesity and polycystic ovarian syndrome. d-chiro-Inositol deficiency exacerbates insulin resistance in the liver, muscles, and fat, while depletion of myo-inositol results in the development of diabetic complications. Cyclitols are successfully applied in treatment of polycystic ovarian syndrome, simultaneous are observed effective reducing of BMI, improving the hormonal profile, and increasing fertility. Moreover, Cyclitols have anti-atherogenic, anti-oxidative, anti-inflammatory, and anti-cancer properties. Conclusion: The properties of Cyclitols may be a good therapeutic option in the reduction of metabolically induced inflammation. Due to well drugs tolerance and low toxicity of these compounds, Cyclitols are recommend for pregnant women and also for children. Another advantage is their widespread presence and easy availability, which encourages their use in medicine.
