scholarly journals Centrifugation-based assay for examining nanoparticle–lipid membrane binding and disruption

The Analyst ◽  
2014 ◽  
Vol 139 (5) ◽  
pp. 973 ◽  
Author(s):  
Aihong Xi ◽  
Geoffrey D. Bothun
Keyword(s):  
Lipid Membrane ◽  
Membrane Binding

scholarly journals Lipid Membrane Binding of Computationally-Designed DNA Aptamers Specific for Phosphatidylserine

2013 ◽  
Vol 104 (2) ◽  
pp. 93a-94a
Author(s):  
Md Ashrafuzzaman ◽  
H.M. Embark ◽  
H.B. Jagirdar ◽  
A. Alsenaidy ◽  
C.Y. Tseng ◽  
...  
Keyword(s):  
Lipid Membrane ◽  
Membrane Binding ◽  
Dna Aptamers

scholarly journals Physicochemical Mechanism for the Lipid Membrane Binding of Polyarginine: The Favorable Enthalpy Change with Structural Transition from Random Coil to α-Helix

2012 ◽  
Vol 41 (10) ◽  
pp. 1374-1376 ◽  
Author(s):  
Yuki Takechi ◽  
Chiharu Mizuguchi ◽  
Masafumi Tanaka ◽  
Toru Kawakami ◽  
Saburo Aimoto ◽  
...  
Keyword(s):  
Structural Transition ◽  
Lipid Membrane ◽  
Membrane Binding ◽  
Enthalpy Change ◽  
Random Coil ◽  
Physicochemical Mechanism ◽  
Α Helix

scholarly journals Interaction of Tarantula Venom Peptide ProTx-II with Lipid Membranes Is a Prerequisite for Its Inhibition of Human Voltage-gated Sodium Channel NaV1.7

2016 ◽  
Vol 291 (33) ◽  
pp. 17049-17065 ◽  
Author(s):  
Sónia Troeira Henriques ◽  
Evelyne Deplazes ◽  
Nicole Lawrence ◽  
Olivier Cheneval ◽  
Stephanie Chaousis ◽  
...  
Keyword(s):  
Sodium Channel ◽  
Binding Site ◽  
Lipid Membranes ◽  
Lipid Membrane ◽  
Membrane Binding ◽  
Voltage Sensor ◽  
Resonance Fluorescence ◽  
Voltage Gated Sodium Channel ◽  
Voltage Gated ◽  
Voltage Sensor Domain

ProTx-II is a disulfide-rich peptide toxin from tarantula venom able to inhibit the human voltage-gated sodium channel 1.7 (hNaV1.7), a channel reported to be involved in nociception, and thus it might have potential as a pain therapeutic. ProTx-II acts by binding to the membrane-embedded voltage sensor domain of hNaV1.7, but the precise peptide channel-binding site and the importance of membrane binding on the inhibitory activity of ProTx-II remain unknown. In this study, we examined the structure and membrane-binding properties of ProTx-II and several analogues using NMR spectroscopy, surface plasmon resonance, fluorescence spectroscopy, and molecular dynamics simulations. Our results show a direct correlation between ProTx-II membrane binding affinity and its potency as an hNaV1.7 channel inhibitor. The data support a model whereby a hydrophobic patch on the ProTx-II surface anchors the molecule at the cell surface in a position that optimizes interaction of the peptide with the binding site on the voltage sensor domain. This is the first study to demonstrate that binding of ProTx-II to the lipid membrane is directly linked to its potency as an hNaV1.7 channel inhibitor.

scholarly journals 3D Packing Defects in Lipid Membrane as a Function of Membrane Order

2019 ◽  
Author(s):  
Madhusmita Tripathy ◽  
Anand Srivastava
Keyword(s):  
Lipid Membrane ◽  
Membrane Binding ◽  
Computationally Efficient ◽  
Protein Motifs ◽  
Liquid Phases ◽  
Preferential Localization ◽  
Peripheral Proteins ◽  
Packing Defects ◽  
3D Packing ◽  
Key Steps

AbstractLipid membrane packing defects are considered as essential parameter that regulates specific membrane binding of several peripheral proteins. In absence of direct experimental characterization, lipid packing defects and their role in the binding of peripheral proteins are generally investigated through computational studies, which have been immensely successful in unraveling the key steps of the membrane-binding process. However, packing defects are calculated using 2-dimensional projections and the crucial information on their depths is generally overlooked. Here we present a simple yet computationally efficient algorithm, which identifies these defects in 3-dimensions. We employ the algorithm to understand the nature of packing defects in flat bilayer membranes exhibiting liquid-ordered (Lo), liquid-disordered (Ld) and co-existing Lo/Ld phases. Our results indicate the presence of shallower and smaller defects in the Lo phase membranes as compared to the defects in Ld and mixed Lo/Ld phase membranes. Such analyses can elucidate the molecular scale mechanisms that drive the preferential localization of certain proteins to either of the liquid phases or their interface. Moreover, on the methodology front, our analyses suggest that the projection based 2-dimensional calculation of packing defects might result in inaccurate quantification of their sizes - a very important feature for membrane association of protein motifs, thus advocating the importance of the 3-dimensional calculations.

Lipid membrane binding of NK-lysin

FEBS Letters ◽  
1998 ◽  
Vol 425 (2) ◽  
pp. 341-344 ◽  
Author(s):  
Jean-Marie Ruysschaert ◽  
Erik Goormaghtigh ◽  
F Homblé ◽  
Mats Andersson ◽  
Edvards Liepinsh ◽  
...  
Keyword(s):  
Lipid Membrane ◽  
Membrane Binding
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