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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Bibliographic Details
Published in:Journal of molecular biology Vol. 349; no. 5; pp. 916 - 921
Main Authors: Kamatari, Yuji O., Yokoyama, Shigeyuki, Tachibana, Hideki, Akasaka, Kazuyuki
Format: Journal Article
Language:English
Published: England Elsevier Ltd 24.06.2005
Subjects:
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
Online Access:Get full text
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Summary: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.
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ISSN:0022-2836
1089-8638
DOI:10.1016/j.jmb.2005.04.010