Pressure-jump NMR Study of Dissociation and Association of Amyloid Protofibrils

The dissociation and reassociation processes of amyloid protofibrils initiated by pressure-jump have been monitored with real-time 1H NMR spectroscopy using an intrinsically denatured disulfide-deficient variant of hen lysozyme. Upon pressure-jump up to 2 kbar, the matured protofibrils grown over se...

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Vydáno v:	Journal of molecular biology Ročník 349; číslo 5; s. 916 - 921
Hlavní autoři:	Kamatari, Yuji O., Yokoyama, Shigeyuki, Tachibana, Hideki, Akasaka, Kazuyuki
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	England Elsevier Ltd 24.06.2005
Témata:	amyloid Amyloid - physiology Amyloid - ultrastructure Animals Chickens dissociation and association kinetics of amyloid protofibrils disulfide-deficient hen lysozyme intrinsically denatured protein Microscopy, Atomic Force Muramidase - physiology Muramidase - ultrastructure Nuclear Magnetic Resonance, Biomolecular Pressure pressure-jump NMR Protein Denaturation Thermodynamics 0SS amyloid pressure-jump NMR AFM intrinsically denatured protein dissociation and association kinetics of amyloid protofibrils disulfide-deficient hen lysozyme
ISSN:	0022-2836, 1089-8638
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Popis
Shrnutí:	The dissociation and reassociation processes of amyloid protofibrils initiated by pressure-jump have been monitored with real-time 1H NMR spectroscopy using an intrinsically denatured disulfide-deficient variant of hen lysozyme. Upon pressure-jump up to 2 kbar, the matured protofibrils grown over several months become fully dissociated into monomers within a few days. Upon pressure-jump down to 30 bar, the dissociated monomers immediately start reassociating. The association and dissociation cycle can be repeated reproducibly by alternating pressure, establishing a notion that the protofibril formation is simply a slow kinetic process toward thermodynamic equilibrium. The outstanding simplicity and effectiveness of pressure in controlling the protofibril formation opens a new route for investigating mechanisms of amyloid fibril-forming reactions. The noted variation in the pressure-induced dissociation rate with the progress of the association reaction suggests multiple mechanisms for the elongation of the protofibril. The disulfide-deficient hen lysozyme offers a particularly simple model system for thermodynamic and kinetic studies of protofibril formation as well as for screening drugs for amyloidosis.
Bibliografie:	ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2
ISSN:	0022-2836 1089-8638
DOI:	10.1016/j.jmb.2005.04.010