Effect of Surfaces on Amyloid Fibril Formation

Moores, Bradley; Drolle, Elizabeth; Attwood, Simon J.; Simons, Janet; Leonenko, Zoya

doi:10.1371/journal.pone.0025954

Cited by 141 publications

(146 citation statements)

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“…Atomic force microscopy (AFM) was used to compare topography and elasticity properties of hepatic plasma membranes. AFM measurements were carried out in a fluid cell (Molecular Imaging) using the Agilent Technologies 5500 Scanning Probe Microscope in tapping mode (MAC mode), as described before (27). Precise force regulation was obtained in MAC mode by using a magnetically coated cantilever (MacLevers Type II from Agilent Technologies; force constant: 2.8 N/m; tip radius: 7 nm, height: 10 -15 m).…”

mentioning

confidence: 99%

Rapid cortisol signaling in response to acute stress involves changes in plasma membrane order in rainbow trout liver

Dindia

Faught

Leonenko

et al. 2013

American Journal of Physiology-Endocrinology and Metabolism

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Dindia L, Faught E, Leonenko Z, Thomas R, Vijayan MM. Rapid cortisol signaling in response to acute stress involves changes in plasma membrane order in rainbow trout liver. Am J Physiol Endocrinol Metab 304: E1157-E1166, 2013. First published March 26, 2013 doi:10.1152/ajpendo.00500.2012.-The activation of genomic signaling in response to stressor-mediated cortisol elevation has been studied extensively in teleosts. However, very little is known about the rapid signaling events elicited by this steroid. We tested the hypothesis that cortisol modulates key stress-related signaling pathways in response to an acute stressor in fish liver. To this end, we investigated the effect of an acute stressor on biophysical properties of plasma membrane and on stressor-related protein phosphorylation in rainbow trout (Oncorhynchus mykiss) liver. A role for cortisol in modulating the acute cellular stress response was ascertained by blocking the stressor-induced elevation of this steroid by metyrapone. The acute stressor exposure increased plasma cortisol levels and liver membrane fluidity (measured by anisotropy of 1,6-diphenyl-1,3,5-hexatriene), but these responses were abolished by metyrapone. Atomic force microscopy further confirmed biophysical alterations in liver plasma membrane in response to stress, including changes in membrane domain topography. The changes in membrane order did not correspond to any changes in membrane fatty acid components after stress, suggesting that changes in membrane structure may be associated with cortisol incorporation into the lipid bilayer. Plasma cortisol elevation poststress correlated positively with activation of intracellular stress signaling pathways, including increased phosphorylation of extracellular signal-related kinases as well as several putative PKA and PKC but not Akt substrate proteins. Together, our results indicate that stressor-induced elevation of plasma cortisol level is associated with alterations in plasma membrane fluidity and rapid activation of stress-related signaling pathways in trout liver. fish; oncorhynchus mykiss; salmonid; glucocorticoid; stress response; membrane fluidity; cell signaling IN RESPONSE TO AN ACUTE STRESSOR, a conserved physiological response is initiated, which involves elevation of stress hormones and subsequent metabolic adjustments, to ensure homeostasis (37). The principal stress hormones, epinephrine and glucocorticoids, have critical functions in the stress adaptation process (9). The fight-or-flight response involves the activation of the sympathetic nervous system, leading to the rapid release of epinephrine from chromaffin cells (9). This catecholamine plays a major role in the acute cardiovascular and metabolic adjustments associated with the fight-or-flight response. The synthesis and release of cortisol, the principal glucocorticoid in teleost, comprises the second phase of the neuroendocrine response, which has a longer-term effect on stress adaptation.

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confidence: 99%

Rapid cortisol signaling in response to acute stress involves changes in plasma membrane order in rainbow trout liver

Dindia

Faught

Leonenko

et al. 2013

American Journal of Physiology-Endocrinology and Metabolism

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“…These techniques are ideally suited to study molecular structure and dynamical properties of membranes 13,21,[39][40][41][42][43][44][45][46] . The approach has advanced significantly during the past decades and is now used to study complex, multi-component membranes and their interaction with drugs, small molecules 13,20,26,37,[47][48][49][50][51][52][53] , bacteria 54,55 , and in particular lipid rafts, i.e. functional lipid domains 16,17,[56][57][58][59][60] .…”

Section: Discussionmentioning

confidence: 99%

The Molecular Structure of Human Red Blood Cell Membranes From Highly Oriented, Solid Supported Multi-Lamellar Membranes

Himbert

Alsop

Rheinstädter

2018

Biophysical Journal

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We prepared highly oriented, multi-lamellar stacks of human red blood cell (RBC) membranes applied on silicon wafers. RBC ghosts were prepared by hemolysis and applied onto functionalized silicon chips and annealed into multi-lamellar RBC membranes. High resolution X-ray diffraction was used to determine the molecular structure of the stacked membranes. We present direct experimental evidence that these RBC membranes consist of nanometer sized domains of integral coiled-coil peptides, as well as liquid ordered (l o ) and liquid disordered (l d ) lipids. Lamellar spacings, membrane and hydration water layer thicknesses, areas per lipid tail and domain sizes were determined. The common drug aspirin was added to the RBC membranes and found to interact with RBC membranes and preferably partition in the head group region of the l o domain leading to a fluidification of the membranes, i.e., a thinning of the bilayers and an increase in lipid tail spacing. Our results further support current models of RBC membranes as patchy structures and provide unprecedented structural details of the molecular organization in the different domains.The presence of pale cells with no internal content in a blood smear is typically indicative of a disease. These cells are produced by hemolysis and have been named red blood cell (RBC) ghosts based on their appearance under the microscope. RBC ghosts can be prepared artificially [1][2][3] . The first published protocol in 1963 by Dodge, Mitchell and Hanahan describes the extraction of the cell membrane from RBCs through hemolysis and was an essential step in the development of membrane proteomics and lipidomics 4,5 . While there is detailed knowledge of the composition of RBC membranes, information about the molecular organization of these components in the actual membranes is scarce 6 . This is, in particular, a consequence of the lack of suitable experimental techniques. The disordered, patchy and highly dynamic state of biological materials impedes, for instance, the use of high-resolution diffraction techniques as in protein crystallography. To overcome this constraint, we prepared highly oriented stacks of RBC membranes on silicon wafers and studied their molecular properties in-vitro using high resolution X-ray diffraction. The results present evidence for nanometer-sized domains of coiled-coils peptides, as well as liquid ordered (l o ) and liquid disordered (l d ) lipid patches, and give a detailed picture of the molecular organization in these domains.When present in the body, aspirin (acetylsalicylic acid, ASA) and its metabolites interact with the cyclo-oxygenase (COX) pathway. The inhibition of both COX isoforms, COX-1 and COX-2, by higher dose aspirin is believed to lead to analgesic and anti-inflammatory effects, while lower doses, sufficient to inhibit COX-1 activity, lead to anti-platelet activity 7,8 . There is recent evidence that membrane composition and fluidity play an important role in platelet cell function [9][10][11] , possibly related to the formation of rafts 12 .

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“…Such a mechanism has practical applications in industrial biosensors, in biotechnology, and in nanotechnology [3,8]. Surface-mediated fibril formation occurs in oligopeptides (typically around 20 residues long) [9][10][11][12] and amyloid beta peptide [13][14][15][16], but also for silkelastine-like polymers [17,18]. The surface-induced fibril selfassembly process can occur via several routes.…”

Section: Introductionmentioning

confidence: 99%

“…The surface-induced fibril selfassembly process can occur via several routes. One involves a nucleation-and-growth process in solution, after which the preformed seed adsorbs on the surface and continues to grow [9][10][11][12][13][14]16,18]. Another is by direct adsorption of the single molecules on the surface [9,15,17,18].…”

Section: Introductionmentioning

confidence: 99%

Competition between surface adsorption and folding of fibril-forming polypeptides

Kleijn

Abeln

et al. 2015

Phys. Rev. E

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Competition between surface adsorption and folding of fibril-forming polypeptidesNi, R.; Kleijn, J.M.; Abeln, S.; Cohen Stuart, M.A.; Bolhuis, P.G. Published in:Physical Review E DOI:10.1103/PhysRevE.91.022711 Link to publication Citation for published version (APA):Ni, R., Kleijn, J. M., Abeln, S., Cohen Stuart, M. A., & Bolhuis, P. G. (2015). Competition between surface adsorption and folding of fibril-forming polypeptides. Physical Review E, 91(2), 022711. DOI: 10.1103/PhysRevE.91.022711 General rightsIt is not permitted to download or to forward/distribute the text or part of it without the consent of the author(s) and/or copyright holder(s), other than for strictly personal, individual use, unless the work is under an open content license (like Creative Commons). Disclaimer/Complaints regulationsIf you believe that digital publication of certain material infringes any of your rights or (privacy) interests, please let the Library know, stating your reasons. In case of a legitimate complaint, the Library will make the material inaccessible and/or remove it from the website. Please Ask the Library: http://uba.uva.nl/en/contact, or a letter to: Library of the University of Amsterdam, Secretariat, Singel 425, 1012 WP Amsterdam, The Netherlands. You will be contacted as soon as possible. Download date: 11 May 2018PHYSICAL REVIEW E 91, 022711 (2015) Competition between surface adsorption and folding of fibril-forming polypeptides Self-assembly of polypeptides into fibrillar structures can be initiated by planar surfaces that interact favorably with certain residues. Using a coarse-grained model, we systematically studied the folding and adsorption behavior of a β-roll forming polypeptide. We find that there are two different folding pathways depending on the temperature: (i) at low temperature, the polypeptide folds in solution into a β-roll before adsorbing onto the attractive surface; (ii) at higher temperature, the polypeptide first adsorbs in a disordered state and folds while on the surface. The folding temperature increases with increasing attraction as the folded β-roll is stabilized by the surface. Surprisingly, further increasing the attraction lowers the folding temperature again, as strong attraction also stabilizes the adsorbed disordered state, which competes with folding of the polypeptide. Our results suggest that to enhance the folding, one should use a weakly attractive surface. They also explain the recent experimental observation of the nonmonotonic effect of charge on the fibril formation on an oppositely charged surface [C.

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Effect of Surfaces on Amyloid Fibril Formation

Cited by 141 publications

References 70 publications

Rapid cortisol signaling in response to acute stress involves changes in plasma membrane order in rainbow trout liver

Rapid cortisol signaling in response to acute stress involves changes in plasma membrane order in rainbow trout liver

The Molecular Structure of Human Red Blood Cell Membranes From Highly Oriented, Solid Supported Multi-Lamellar Membranes

Competition between surface adsorption and folding of fibril-forming polypeptides

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