Relevant bibliographies by topics / Trehalase inhibitors

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Academic literature on the topic 'Trehalase inhibitors'

Author: Grafiati
Published: 9 March 2023
Last updated: 10 March 2023

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Journal articles on the topic "Trehalase inhibitors"

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White, Christopher, Deborah B. Lee, and Stephen J. Free. "NEUROSPORA TREHALASE AND ITS STRUCTURAL GENE." Genetics 110, no. 2 (June 1, 1985): 217–27. http://dx.doi.org/10.1093/genetics/110.2.217.

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ABSTRACT We have isolated Neurospora trehalaseless mutants and mapped the trehalase structural gene to linkage group I. The structural gene mutations not only affect thermostability and other characteristics of the enzyme but also affect the production of an inhibitor of the wild-type trehalase. The inhibitor appears to be the mutant trehalase. We suggest that the mutant subunits act as inhibitors by entering into the multimeric forms of the enzyme and altering the ability of the normal wild-type subunits to catalyze the cleavage of trehalose.—Wild type trehalase has been purified to near homogeneity, and its characteristics have been studied. It was purified as a tetramer, with each subunit having a molecular weight of 88,000.—We have studied the regulation of trehalase and found the production of trehalase to be glucose repressible. Cells begin to produce trehalase 60 min after being transferred to glucose-free medium.
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Matassini, Camilla, Camilla Parmeggiani, and Francesca Cardona. "New Frontiers on Human Safe Insecticides and Fungicides: An Opinion on Trehalase Inhibitors." Molecules 25, no. 13 (July 1, 2020): 3013. http://dx.doi.org/10.3390/molecules25133013.

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In the era of green economy, trehalase inhibitors represent a valuable chance to develop non-toxic pesticides, being hydrophilic compounds that do not persist in the environment. The lesson on this topic that we learned from the past can be of great help in the research on new specific green pesticides. This review aims to describe the efforts made in the last 50 years in the evaluation of natural compounds and their analogues as trehalase inhibitors, in view of their potential use as insecticides and fungicides. Specifically, we analyzed trehalase inhibitors based on sugars and sugar mimics, focusing on those showing good inhibition properties towards insect trehalases. Despite their attractiveness as a target, up to now there are no trehalase inhibitors that have been developed as commercial insecticides. Although natural complex pseudo di- and trisaccharides were firstly studied to this aim, iminosugars look to be more promising, showing an excellent specificity profile towards insect trehalases. The results reported here represent an overview and a discussion of the best candidates which may lead to the development of an effective insecticide in the future.
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Marten, Andrew D., Alicyn I. Stothard, Karishma Kalera, Benjamin M. Swarts, and Michael J. Conway. "Validamycin A Delays Development and Prevents Flight in Aedes aegypti (Diptera: Culicidae)." Journal of Medical Entomology 57, no. 4 (January 26, 2020): 1096–103. http://dx.doi.org/10.1093/jme/tjaa004.

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Abstract Trehalose is a disaccharide that is the major sugar found in insect hemolymph fluid. Trehalose provides energy, and promotes growth, metamorphosis, stress recovery, chitin synthesis, and insect flight. The hydrolysis of trehalose is under the enzymatic control of the enzyme trehalase. Trehalase is critical to the role of trehalose in insect physiology, and is required for the regulation of metabolism and glucose generation. Trehalase inhibitors represent a novel class of insecticides that have not been fully developed. Here, we tested the ability of trehalose analogues to function as larvacides or adulticides in an important disease vector—Aedes aegypti. We show that validamycin A, but not 5-thiotrehalose, delays larval and pupal development and prevents flight of adult mosquitoes. Larval mosquitoes treated with validamycin A were hypoglycemic and pupae had increased levels of trehalose. Treatment also skewed the sex ratio toward male mosquitoes. These data reveal that validamycin A is a mosquito adulticide that can impair normal development of an important disease vector.
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Streeter, J. G., and M. L. Gomez. "Three Enzymes for Trehalose Synthesis in Bradyrhizobium Cultured Bacteria and in Bacteroids from Soybean Nodules." Applied and Environmental Microbiology 72, no. 6 (June 2006): 4250–55. http://dx.doi.org/10.1128/aem.00256-06.

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ABSTRACT α,α-Trehalose is a disaccharide accumulated by many microorganisms, including rhizobia, and a common role for trehalose is protection of membrane and protein structure during periods of stress, such as desiccation. Cultured Bradyrhizobium japonicum and B. elkanii were found to have three enzymes for trehalose synthesis: trehalose synthase (TS), maltooligosyltrehalose synthase (MOTS), and trehalose-6-phosphate synthetase. The activity level of the latter enzyme was much higher than those of the other two in cultured bacteria, but the reverse was true in bacteroids from nodules. Although TS was the dominant enzyme in bacteroids, the source of maltose, the substrate for TS, is not clear; i.e., the maltose concentration in nodules was very low and no maltose was formed by bacteroid protein preparations from maltooligosaccharides. Because bacteroid protein preparations contained high trehalase activity, it was imperative to inhibit this enzyme in studies of TS and MOTS in bacteroids. Validamycin A, a commonly used trehalase inhibitor, was found to also inhibit TS and MOTS, and other trehalase inhibitors, such as trehazolin, must be used in studies of these enzymes in nodules. The results of a survey of five other species of rhizobia indicated that most species sampled had only one major mechanism for trehalose synthesis. The presence of three totally independent mechanisms for the synthesis of trehalose by Bradyrhizobium species suggests that this disaccharide is important in the function of this organism both in the free-living state and in symbiosis.
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KAMEDA, YUKIHIKO, NAOKI ASANO, TAKUJI YAMAGUCHI, and KATSUHIKO MATSUI. "Validoxylamines as trehalase inhibitors." Journal of Antibiotics 40, no. 4 (1987): 563–65. http://dx.doi.org/10.7164/antibiotics.40.563.

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Bini, Davide, Francesca Cardona, Matilde Forcella, Camilla Parmeggiani, Paolo Parenti, Francesco Nicotra, and Laura Cipolla. "Synthesis and biological evaluation of nojirimycin- and pyrrolidine-based trehalase inhibitors." Beilstein Journal of Organic Chemistry 8 (April 5, 2012): 514–21. http://dx.doi.org/10.3762/bjoc.8.58.

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A small set of nojirimycin- and pyrrolidine-based iminosugar derivatives has been synthesized and evaluated as potential inhibitors of porcine and insect trehalases. Compounds 12, 13 and 20 proved to be active against both insect and porcine trehalases with selectivity towards the insect glycosidase, while compounds 10, 14 and 16 behaved as inhibitors only of insect trehalase. Despite the fact that the activity was found in the micromolar range, these findings may help in elucidating the structural features of this class of enzymes of different origin, which are still scarcely characterised.
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Kyosseva, S. V., Z. N. Kyossev, and A. D. Elbein. "Inhibitors of Pig Kidney Trehalase." Archives of Biochemistry and Biophysics 316, no. 2 (February 1995): 821–26. http://dx.doi.org/10.1006/abbi.1995.1110.

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QIAN, XUHONG, ZHIBIN LI, ZHI LIU, GONGHUA SONG, and ZHONG LI. "Syntheses of 2-Aryliminooxazolidine Derivatives as Trehalase Inhibitors." Journal of Antibiotics 54, no. 12 (2001): 1108–10. http://dx.doi.org/10.7164/antibiotics.54.1108.

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Gibson, Robert P, Tracey M Gloster, Shirley Roberts, R. Anthony J Warren, Isabel Storch de Gracia, Ángela García, Jose L Chiara, and Gideon J Davies. "Molecular Basis for Trehalase Inhibition Revealed by the Structure of Trehalase in Complex with Potent Inhibitors." Angewandte Chemie 119, no. 22 (May 25, 2007): 4193–97. http://dx.doi.org/10.1002/ange.200604825.

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Gibson, Robert P, Tracey M Gloster, Shirley Roberts, R. Anthony J Warren, Isabel Storch de Gracia, Ángela García, Jose L Chiara, and Gideon J Davies. "Molecular Basis for Trehalase Inhibition Revealed by the Structure of Trehalase in Complex with Potent Inhibitors." Angewandte Chemie International Edition 46, no. 22 (May 25, 2007): 4115–19. http://dx.doi.org/10.1002/anie.200604825.

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Dissertations / Theses on the topic "Trehalase inhibitors"

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BINI, DAVIDE. "Synthesis of Glycoconjugates and their Analogs for the Study of Biological Systems." Doctoral thesis, Università degli Studi di Milano-Bicocca, 2016. http://hdl.handle.net/10281/103143.

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ABSTRACT The project was focussed on the development of three main topics: a) trehalose mimics as trehalase inhibitors, b) synthesis of multivalent glycoconjugates and c) synthesis of glycosylated Pluronic block copolymers. a) Trehalose mimics as trehalase inhibitors Trehalase (α-glucoside-1-glucohydrolase, EC 3.2.1.28) is a specific glycosidase that catalyzes the hydrolysis of trehalose (α-D-glucopyranosyl-α-D-glucopyranoside) to the two constituent glucose units. This disaccharide is found in many organisms, but is absent in mammals. In insects, trehalose hydrolysis by trehalase is fundamental in various physiological processes. Given these premises, insect trehalases are attractive targets for the search of inhibitors as potential novel and selective insecticides. The aim of the project is the design, synthesis and in vitro and in vivo biological evaluation of some trehalose mimics (iminosugars or polyhydroxylated pyrrolizidine alkaloids) as selective insect trehalases inhibitors. b) Synthesis of multivalent glycoconjugates Recognition processes between glycans and their receptors are of paramount relevance in several biological phenomena, both in physiological and in pathological conditions. Moreover, most often these binding events occur in a multivalent and cooperative manner. In order to better understand these phenomena, dendrimers and dendrons have been developed to provide multivalent glycoconjugates. The aim of the project is the design and synthesis of new hetrobifunctional dendrons for carbohydrates multivalent presentation, and the study of synthetized glycoconjugates interactions with specific proteins. c) Synthesis of glycosylated Pluronic block copolymers Polymer-based nanotechnology became one of the most attractive and fast growing areas of pharmaceutical research. One promising example of such polymer nanomaterials is represented by a class of Pluronic block copolymers. In aqueous solutions, at concentrations above critical micelle concentration, these copolymers self-assemble into micelles. In application to anticancer chemotherapy, low molecular mass drugs encapsulation in micelles can diminish drug extravasation into normal tissues and provide for a passive drug targeting to tumors via the enhanced permeability and retention (EPR) effect. In order to gain also an active targeting effect on Pluronic micelles, I have been working on the design and synthesis of new glycosylated Pluronic block copolymers for antitumor drug delivery.
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Thanna, Sandeep. "Design and Synthesis of Novel Inhibitors for Enzymatic Targets in Trehalose Utilization Pathways of Mycobacterium tuberculosis." University of Toledo / OhioLINK, 2017. http://rave.ohiolink.edu/etdc/view?acc_num=toledo1501627900249048.

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Huang, Yin-Jung, and 黃胤榮. "Functional expression of human trehalase in Escherichia coli and identification of novel trehalase inhibitors." Thesis, 2013. http://ndltd.ncl.edu.tw/handle/95603406888333667888.

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碩士
國立臺灣師範大學
生命科學研究所
101
In mammals, trehalase, sucrase-isomaltase and maltase-glucoamylase are the major α-glycosidases of the intestinal brush border membranes. These enzymes are responsible for the degradation of di- and oligosaccharides into monosaccharides, and are crucial for the energy-intake. Trehalase (EC 3.2.1.28) hydrolyses α,α-trehalose (1-α-D-glucopyranosyl α-D-glucopyranoside) to two glucose molecules. The intestinal trehalase is involved in the hydrolysis of ingested trehalose which is found mainly in many nutrient foods. The dual protective properties of trehalose (as a chemical chaperone and an inducer of autophagy) have encouraged pharmaceutical application of the disaccharide in neurodegenerative diseases caused by protein aggregation process. Therefore, it is theoretically possible to increase intestinal absorption of trehalose through inhibiting intestinal trehalase activity, and thus increase in trehalose content in blood or brain. This may in turn alleviate neurological protein deposition diseases. The protein structure, catalytic mechanism and specific inhibitors of human intestinal trehalase (hTreH) have not been elucidated. In the present study, a cDNA fragment encoding the mature form of hTreH was cloned and recombinant hTreH was expressed in Escherichia coli. However,the recombinant hTreH was expressed as an inclusion body. Protein refolding through dialysis and on-column refolding process were performed. The refolded enzyme showed very low specific activity. To prevent protein misfolding through the formation of incorrect intra- or inter-molecular disulfide bonds and thus increase its solubility, based on tertiary structure modeling, several predicted non-disulfide-bonding cysteine residues in hTreH were replaced with serine by site-directed mutagenesis. Four cysteine residues in hTreH were changed into serine, which are predicted to be distant from each other and may not form disulfide bonds with each other. However, the mutant proteins were also expressed as inclusion bodies, and the refolded enzymes still showed no activity. Several trehalose analogs were biochemically characterized as mammalian trehalase inhibitors, and they can be as potential therapeutics for the protein deposition-mediated diseases. Keyword: trehalose, trehalase, trehalase inhibitor, recombinant protein expression
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Miao, Yi. "Structural and Biochemical Dissection of the Trehalose Biosynthetic Complex in Pathogenic Fungi." Diss., 2016. http://hdl.handle.net/10161/12130.

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Trehalose is a non-reducing disaccharide essential for pathogenic fungal survival and virulence. The biosynthesis of trehalose requires the trehalose-6-phosphate synthase, Tps1, and trehalose-6-phosphate phosphatase, Tps2. More importantly, the trehalose biosynthetic pathway is absent in mammals, conferring this pathway as an ideal target for antifungal drug design. However, lack of germane biochemical and structural information hinders antifungal drug design against these targets.

In this dissertation, macromolecular X-ray crystallography and biochemical assays were employed to understand the structures and functions of proteins involved in the trehalose biosynthetic pathway. I report here the first eukaryotic Tps1 structures from Candida albicans (C. albicans) and Aspergillus fumigatus (A. fumigatus) with substrates or substrate analogs. These structures reveal the key residues involved in substrate binding and catalysis. Subsequent enzymatic assays and cellular assays highlight the significance of these key Tps1 residues in enzyme function and fungal stress response. The Tps1 structure captured in its transition-state with a non-hydrolysable inhibitor demonstrates that Tps1 adopts an “internal return like” mechanism for catalysis. Furthermore, disruption of the trehalose biosynthetic complex formation through abolishing Tps1 dimerization reveals that complex formation has regulatory function in addition to trehalose production, providing additional targets for antifungal drug intervention.

I also present here the structure of the Tps2 N-terminal domain (Tps2NTD) from C. albicans, which may be involved in the proper formation of the trehalose biosynthetic complex. Deletion of the Tps2NTD results in a temperature sensitive phenotype. Further, I describe in this dissertation the structures of the Tps2 phosphatase domain (Tps2PD) from C. albicans, A. fumigatus and Cryptococcus neoformans (C. neoformans) in multiple conformational states. The structures of the C. albicans Tps2PD -BeF3-trehalose complex and C. neoformans Tps2PD(D24N)-T6P complex reveal extensive interactions between both glucose moieties of the trehalose involving all eight hydroxyl groups and multiple residues of both the cap and core domains of Tps2PD. These structures also reveal that steric hindrance is a key underlying factor for the exquisite substrate specificity of Tps2PD. In addition, the structures of Tps2PD in the open conformation provide direct visualization of the conformational changes of this domain that are effected by substrate binding and product release.

Last, I present the structure of the C. albicans trehalose synthase regulatory protein (Tps3) pseudo-phosphatase domain (Tps3PPD) structure. Tps3PPD adopts a haloacid dehydrogenase superfamily (HADSF) phosphatase fold with a core Rossmann-fold domain and a α/β fold cap domain. Despite lack of phosphatase activity, the cleft between the Tps3PPD core domain and cap domain presents a binding pocket for a yet uncharacterized ligand. Identification of this ligand could reveal the cellular function of Tps3 and any interconnection of the trehalose biosynthetic pathway with other cellular metabolic pathways.

Combined, these structures together with significant biochemical analyses advance our understanding of the proteins responsible for trehalose biosynthesis. These structures are ready to be exploited to rationally design or optimize inhibitors of the trehalose biosynthetic pathway enzymes. Hence, the work described in this thesis has laid the groundwork for the design of Tps1 and Tps2 specific inhibitors, which ultimately could lead to novel therapeutics to treat fungal infections.


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Book chapters on the topic "Trehalase inhibitors"

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El Nemr, Ahmed, and El Sayed H. El Ashry. "Potential trehalase inhibitors." In Advances in Carbohydrate Chemistry and Biochemistry, 45–114. Elsevier, 2011. http://dx.doi.org/10.1016/b978-0-12-385520-6.00003-0.

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