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The interaction of amyloid A beta(1-40) with lipid bilayers and ganglioside as studied by P-31 solid-state NMR
Amyloid P-peptide (A beta) is a major component of plaques in Alzheimer's disease, and formation of senile plaques has been suggested to originate fro m regions of neuronal membrane rich in gangliosides. We analyzed the mode of interaction of A beta with lipid bilayers by multinuclear NMR using P-31 nuclei. We found that A beta (1-40) strongly perturbed the bilayer structure of dimyristoylphosphatidylcholine (DMPQ, to form a non-lamellar phase (most likely micellar). The ganglioside GM1 potentiated the effect of A beta (1-40), as viewed from P-31 NMR. The difference of the isotropic peak intensity between DMPC/A beta and DMPC/GM1/A beta suggests a specific interaction between A beta and GM1. We show that in the DMPC/GM1/A beta system there are three lipid phases, namely a lamellar phase, a hexagonal phase and non-oriented lipids. The latter two phases are induced by the presence of the A beta peptide, and facilitated by GM1. 9) 2008 Elsevier Ireland Ltd. All rights reserved
Erratum
Nighttime temperature treatment of fruit clusters of 'Ald Queen' grapes during maturation and its effects ofn the sldn color and abscisic acid contentVitis 46 (4), 208-209 (2007
Entropic torque
Quantitative predictions are presented of a depletion-induced torque and
force acting on a single colloidal hard rod immersed in a solvent of hard
spheres close to a planar hard wall. This torque and force, which are entirely
of entropic origin, may play an important role for the key-lock principle,
where a biological macromolecule (the key) is only functional in a particular
orientation with respect to a cavity (the lock)
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