Determination of Peptide Oligomerization in Lipid Bilayers Using19F Spin Diffusion NMR

The basic principles underlying fluctuation phenomena in thermodynamics have long been understood (for reviews see Kubo, 1957; Kubo, Matsuo & Kazuhiro 1973 Lax, 1960). Classical examples of how fluctuation analysis can provide an insight into the corpuscular nature of matter are the determination of Avogadro's number according to Einstein's theory of Brownian motion (see, e.g. Uhlenbeck & Ornstein, 1930; Kac, 1947) and the evaluation of the electronic charge from the shot noise in vacuum tubes (see Van der Ziel, 1970).

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The essential role of lipid bilayers in the determination of stratum corneum permeability

International Journal of Pharmaceutics ◽

10.1016/0378-5173(91)90230-l ◽

1991 ◽

Vol 74 (2-3) ◽

pp. 137-146 ◽

Cited By ~ 10

Author(s):

Anthony J.I. Ward ◽

Charles du Reau

Keyword(s):

Stratum Corneum ◽

Lipid Bilayers ◽

Essential Role

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Segmental dynamic heterogeneity of short-chain grafted-poly(dimethylsiloxane) by 1H spin-diffusion NMR

Chemical Physics Letters ◽

10.1016/j.cplett.2006.09.092 ◽

2006 ◽

Vol 431 (4-6) ◽

pp. 404-409 ◽

Cited By ~ 3

Author(s):

Marko Bertmer ◽

Dan E. Demco ◽

Mingfei Wang ◽

Claudiu Melian ◽

Ramona I. Marcean-Chelcea ◽

...

Keyword(s):

Spin Diffusion ◽

Short Chain ◽

Dynamic Heterogeneity ◽

Diffusion Nmr ◽

Segmental Dynamic

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Structural, functional and computational studies of membrane recognition by Plasmodium Perforin-Like Proteins 1 and 2.

10.1101/2021.12.16.473088 ◽

2021 ◽

Author(s):

Sophie Williams ◽

Xiulian Yu ◽

Tao Ni ◽

Robert Gilbert ◽

Phillip Stansfeld

Keyword(s):

Life Cycle ◽

Lipid Bilayers ◽

Membrane Binding ◽

Binding Activity ◽

Life Cycles ◽

Site Directed Mutagenesis ◽

Parasite Life Cycle ◽

Dynamics Simulations ◽

Membrane Recognition

Perforin-like proteins (PLPs) play key roles in the mechanisms associated with parasitic disease caused by apicomplexans such as Plasmodium (malaria) and Toxoplasma. The T. gondii PLP1 (TgPLP1) mediates tachyzoite egress from cells, while the five Plasmodium PLPs carry out various roles in the life cycle of the parasite and with respect to the molecular basis of disease. Here we focus on Plasmodium vivax PLP1 and PLP2 (PvPLP1 and PvPLP2) compared to TgPLP1; PvPLP1 is important for invasion of mammalian hosts by the parasite and establishment of a chronic infection, PvPLP2 is important during the symptomatic blood stage of the parasite life cycle. Determination of the crystal structure of the membrane-binding APCβ domain of PvPLP1 reveals notable differences with that of TgPLP1, which are reflected in its inability to bind lipid bilayers in the way that TgPLP1 and PvPLP2 can be shown to. Molecular dynamics simulations combined with site-directed mutagenesis and functional assays allow a dissection of the binding interactions of TgPLP1 and PvPLP2 on lipid bilayers, and reveal a similar tropism for lipids found enriched in the inner leaflet of the mammalian plasma membrane. In addition to this shared mode of membrane binding PvPLP2 displays a secondary synergistic interaction side-on from its principal bilayer interface. This study underlines the substantial differences between the biophysical properties of the APCβ domains of Apicomplexan PLPs, which reflect their significant sequence diversity. Such differences will be important factors in determining the cell targeting and membrane-binding activity of the different proteins, in their different developmental roles within parasite life cycles.

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