Sterols and membrane dynamics

Dufourc, Érick J.

doi:10.1007/s12154-008-0010-6

Cited by 373 publications

(316 citation statements)

References 45 publications

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“…The membranes themselves are complex mixtures of various phospholipids and other molecules such as sterols (mainly cholesterol) [3], sphingolipids [2] and glycolipids [4]. In addition, numerous membrane proteins provide ion channels, pores and points of signal transduction across the membrane [2].…”

Section: Introductionmentioning

confidence: 99%

Monitoring changes of paramagnetically-shifted 31P signals in phospholipid vesicles

Joyce

Williams

Serpell

et al. 2016

Chemical Physics Letters

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Phospholipid vesicles are commonly used as biomimetics in the investigation of the interaction of various species with cell membranes. In this paper we present a 31 P NMR investigation of a simple vesicle system using a paramagnetic shift reagent to probe the inner and outer layers of the lipid bilayer. Time-dependent changes in the 31 P NMR signal are observed, which differ whether the paramagnetic species is inside or outside the vesicle, and on the choice of buffer solution used. An interpretation of these results is given in terms of the interaction of the paramagnetic shift reagent with the lipids.3

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Section: Introductionmentioning

confidence: 99%

Monitoring changes of paramagnetically-shifted 31P signals in phospholipid vesicles

Joyce

Williams

Serpell

et al. 2016

Chemical Physics Letters

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“…Assuming that lipid bilayers constitute about 10% of the cell mass (Alberts, 2015), the measured concentration of 18 mg g 21 celastrol in orange Tripterygium roots would translate into a concentration of 180 mg g 21 in membranes. Considering the fact that triterpenoids accumulate only in the periderm (which constitutes about 20% of the volume of orange roots), the concentration in this layer would be 900 mg g 21 (corresponding to 90 mass %), which is considerably more than the highest concentrations estimated for the plant plasma membrane (50 mass %; Dufourc, 2008). Therefore, one would have to postulate that celastrol replaces other sterols in the plasma membrane of Tripterygium periderm cells.…”

Section: How Are Triterpenoids Sequestered Within Periderm Cells?mentioning

confidence: 97%

Integrative Approaches for the Identification and Localization of Specialized Metabolites in Tripterygium Roots

et al. 2016

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ORCID IDs: 0000-0001-6565-9584 (B.M.L.); 0000-0001-7934-7987 (N.S.); 0000-0002-0600-6847 (D.Š.).Members of the genus Tripterygium are known to contain an astonishing diversity of specialized metabolites. The lack of authentic standards has been an impediment to the rapid identification of such metabolites in extracts. We employed an approach that involves the searching of multiple, complementary chromatographic and spectroscopic data sets against the Spektraris database to speed up the metabolite identification process. Mass spectrometry-based imaging indicated a differential localization of triterpenoids to the periderm and sesquiterpene alkaloids to the cortex layer of Tripterygium roots. We further provide evidence that triterpenoids are accumulated to high levels in cells that contain suberized cell walls, which might indicate a mechanism for storage. To our knowledge, our data provide first insights into the cell type specificity of metabolite accumulation in Tripterygium and set the stage for furthering our understanding of the biological implications of specialized metabolites in this genus.

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“…A further difference between mammalian and bacterial cell membranes is the increased presence of sterols, which regulate membrane fluidity and potentially prevent the disruption by AMPs and their mimics. 8 Different mechanisms have been observed for the membrane disruption of AMPs, with the barrel stave model (i.e. alamethicin 9 ), the toroidal pore model (i.e.…”

Section: Amphiphilic Balancementioning

confidence: 99%

Antimicrobial Polymers: Mimicking Amino Acid Functionali ty, Sequence Control and Three-dimensional Structure of Host-defen se Peptides

Hartlieb

Williams

Kuroki

et al. 2017

CMC

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(2017) Antimicrobial polymers : mimicking amino acid functionality, sequence control and threedimensional structure of host-defense peptides. Current Medicinal Chemistry, 24 . Permanent WRAP URL:http://wrap.warwick.ac.uk/88727 Copyright and reuse:The Warwick Research Archive Portal (WRAP) makes this work by researchers of the University of Warwick available open access under the following conditions. Copyright © and all moral rights to the version of the paper presented here belong to the individual author(s) and/or other copyright owners. To the extent reasonable and practicable the material made available in WRAP has been checked for eligibility before being made available.Copies of full items can be used for personal research or study, educational, or not-for-profit purposes without prior permission or charge. Provided that the authors, title and full bibliographic details are credited, a hyperlink and/or URL is given for the original metadata page and the content is not changed in any way. Publisher's statement:The published manuscript is available at EurekaSelect via http://www.eurekaselect.com/149294/article A note on versions:The version presented here may differ from the published version or, version of record, if you wish to cite this item you are advised to consult the publisher's version. Please see the 'permanent WRAP URL' above for details on accessing the published version and note that access may require a subscription. Abstract: Peptides and proteins control and direct all aspects of cellular function and communication.Having been honed by nature for millions of years, they also typically display an unsurpassed specificity for their biological targets. This underlies the continued focus on peptides as promising drug candidates. However, the development of peptides into viable drugs is hampered by their lack of chemical and pharmacokinetic stability and the cost of large scale production. One method to overcome such hindrances is to develop polymer systems that are able to retain the important structural features of these biologically active peptides, while being cheaper and easier to produce and manipulate chemically.This review illustrates these principles using examples of polymers designed to mimic antimicrobial host-defence peptides. The host-defence peptides have been identified as some of the most important leads for the next generation of antibiotics as they typically exhibit broad spectrum antimicrobial ability, low toxicity toward human cells and little susceptibility to currently known mechanisms of bacterial resistance. Their movement from the bench to clinic is yet to be realised, however, due to the limitations of these peptides as drugs. The literature provides a number of examples of polymers that have been able to mimic these peptides through all levels of structure, starting from specific amino acid sidechains, through to more global features such as overall charge, molecular weight and three-dimensional structure (e.g. α-helical). The resulting optimised polymers are able ret...

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Sterols and membrane dynamics

Cited by 373 publications

References 45 publications

Monitoring changes of paramagnetically-shifted 31P signals in phospholipid vesicles

Monitoring changes of paramagnetically-shifted 31P signals in phospholipid vesicles

Integrative Approaches for the Identification and Localization of Specialized Metabolites in Tripterygium Roots

Antimicrobial Polymers: Mimicking Amino Acid Functionali ty, Sequence Control and Three-dimensional Structure of Host-defen se Peptides

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