Distinct Helix Propensities and Membrane Interactions of Human and Rat IAPP1–19 Monomers in Anionic Lipid Bilayers

2015 ◽  
Vol 119 (8) ◽  
pp. 3366-3376 ◽  
Author(s):  
Cong Guo ◽  
Sébastien Côté ◽  
Normand Mousseau ◽  
Guanghong Wei
Keyword(s):  
Lipid Bilayers ◽  
Membrane Interactions ◽  
Anionic Lipid

Fluid or gel phase lipid bilayers to study peptide-membrane interactions?

1996 ◽  
Vol 25 (1) ◽  
pp. 55-59 ◽  
Author(s):  
T. Pott ◽  
J. Dufourcq ◽  
E. J. Dufourc
Keyword(s):  
Lipid Bilayers ◽  
Membrane Interactions ◽  
Gel Phase

scholarly journals Polycation–Anionic Lipid Membrane Interactions

Langmuir ◽  
2020 ◽  
Vol 36 (42) ◽  
pp. 12435-12450
Author(s):  
Wojciech Kopec ◽  
Agata Żak ◽  
Dorota Jamróz ◽  
Rina Nakahata ◽  
Shin-ichi Yusa ◽  
...  
Keyword(s):  
Lipid Membrane ◽  
Membrane Interactions ◽  
Anionic Lipid

scholarly journals Vaccinia Virus Interactions with the Cell Membrane Studied by New Chromatic Vesicle and Cell Sensor Assays

2006 ◽  
Vol 81 (3) ◽  
pp. 1140-1147 ◽  
Author(s):  
Z. Orynbayeva ◽  
S. Kolusheva ◽  
N. Groysman ◽  
N. Gavrielov ◽  
L. Lobel ◽  
...  
Keyword(s):  
Cell Surface ◽  
Vaccinia Virus ◽  
Lipid Bilayers ◽  
Growth Factor Receptor ◽  
Viral Envelope ◽  
Virus Infectivity ◽  
Membrane Interactions ◽  
Viral Interactions ◽  
Epidermal Growth ◽  
Virus Interactions

ABSTRACT The potential danger of cross-species viral infection points to the significance of understanding the contributions of nonspecific membrane interactions with the viral envelope compared to receptor-mediated uptake as a factor in virus internalization and infection. We present a detailed investigation of the interactions of vaccinia virus particles with lipid bilayers and with epithelial cell membranes using newly developed chromatic biomimetic membrane assays. This analytical platform comprises vesicular particles containing lipids interspersed within reporter polymer units that emit intense fluorescence following viral interactions with the lipid domains. The chromatic vesicles were employed as membrane models in cell-free solutions and were also incorporated into the membranes of epithelial cells, thereby functioning as localized membrane sensors on the cell surface. These experiments provide important insight into membrane interactions with and fusion of virions and the kinetic profiles of these processes. In particular, the data emphasize the significance of cholesterol/sphingomyelin domains (lipid rafts) as a crucial factor promoting bilayer insertion of the viral particles. Our analysis of virus interactions with polymer-labeled living cells exposed the significant role of the epidermal growth factor receptor in vaccinia virus infectivity; however, the data also demonstrated the existence of additional non-receptor-mediated mechanisms contributing to attachment of the virus to the cell surface and its internalization.

scholarly journals Effect of Dengue Fusion Peptide in Anionic Lipid Bilayers

2015 ◽  
Vol 108 (2) ◽  
pp. 239a
Author(s):  
Thaís F. Schmidt ◽  
Karin A. Riske
Keyword(s):  
Lipid Bilayers ◽  
Fusion Peptide ◽  
Anionic Lipid

scholarly journals Binding Orientations and Lipid Interactions of Human Amylin at Zwitterionic and Anionic Lipid Bilayers

2016 ◽  
Vol 2016 ◽  
pp. 1-13 ◽  
Author(s):  
Zhenyu Qian ◽  
Yan Jia ◽  
Guanghong Wei
Keyword(s):  
Lipid Bilayers ◽  
Helical Structure ◽  
Terminal Region ◽  
Islet Amyloid ◽  
Anionic Lipid ◽  
Multiple Binding ◽  
Preferential Binding ◽  
Dynamics Simulations ◽  
Binding Orientations ◽  
Human Amylin

Increasing evidence suggests that the interaction of human islet amyloid polypeptide (hIAPP) with lipids may facilitate hIAPP aggregation and cause the death of pancreatic isletβ-cells. However, the detailed hIAPP-membrane interactions and the influences of lipid compositions are unclear. In this study, as a first step to understand the mechanism of membrane-mediated hIAPP aggregation, we investigate the binding behaviors of hIAPP monomer at zwitterionic palmitoyloleoyl-phosphatidylcholine (POPC) bilayer by performing atomistic molecular dynamics simulations. The results are compared with those of hIAPP at anionic palmitoyloleoyl-phosphatidylglycerol (POPG) bilayers. We find that the adsorption of hIAPP to POPC bilayer is mainly initiated from the C-terminal region and the peptide adopts a helical structure with multiple binding orientations, while the adsorption to POPG bilayer is mostly initiated from the N-terminal region and hIAPP displays one preferential binding orientation, with its hydrophobic residues exposed to water. hIAPP monomer inserts into POPC lipid bilayers more readily than into POPG bilayers. Peptide-lipid interaction analyses show that the different binding features of hIAPP at POPC and POPG bilayers are attributed to different magnitudes of electrostatic and hydrogen-bonding interactions with lipids. This study provides mechanistic insights into the different interaction behaviors of hIAPP with zwitterionic and anionic lipid bilayers.

scholarly journals Structural basis of membrane disruption and cellular toxicity by α-synuclein oligomers

Science ◽  
2017 ◽  
Vol 358 (6369) ◽  
pp. 1440-1443 ◽  
Author(s):  
Giuliana Fusco ◽  
Serene W. Chen ◽  
Philip T. F. Williamson ◽  
Roberta Cascella ◽  
Michele Perni ◽  
...  
Keyword(s):  
Lipid Bilayers ◽  
Neurodegenerative Disorders ◽  
Cortical Neurons ◽  
Neuroblastoma Cells ◽  
Structural Basis ◽  
Membrane Disruption ◽  
Membrane Interactions ◽  
Primary Cortical Neurons ◽  
Cellular Toxicity ◽  
Structural Methods

Oligomeric species populated during the aggregation process of α-synuclein have been linked to neuronal impairment in Parkinson’s disease and related neurodegenerative disorders. By using solution and solid-state nuclear magnetic resonance techniques in conjunction with other structural methods, we identified the fundamental characteristics that enable toxic α-synuclein oligomers to perturb biological membranes and disrupt cellular function; these include a highly lipophilic element that promotes strong membrane interactions and a structured region that inserts into lipid bilayers and disrupts their integrity. In support of these conclusions, mutations that target the region that promotes strong membrane interactions by α-synuclein oligomers suppressed their toxicity in neuroblastoma cells and primary cortical neurons.

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