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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Vydané v:	Journal of molecular biology Ročník 349; číslo 5; s. 916 - 921
Hlavní autori:	Kamatari, Yuji O., Yokoyama, Shigeyuki, Tachibana, Hideki, Akasaka, Kazuyuki
Médium:	Journal Article
Jazyk:	English
Vydavateľské údaje:	England Elsevier Ltd 24.06.2005
Predmet:	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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Abstract	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.
AbstractList	The dissociation and reassociation processes of amyloid protofibrils initiated by pressure-jump have been monitored with real-time (1)H 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.The dissociation and reassociation processes of amyloid protofibrils initiated by pressure-jump have been monitored with real-time (1)H 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. The dissociation and reassociation processes of amyloid protofibrils initiated by pressure-jump have been monitored with real-time (1)H 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. 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. The dissociation and reassociation processes of amyloid protofibrils initiated by pressure-jump have been monitored with real-time super(1)H NMR spectroscopy using an intrinsically denatured disulfide-deficient variant of hen lysozyme. Upon pressure-jump up to 2kbar, the matured protofibrils grown over several months become fully dissociated into monomers within a few days. Upon pressure-jump down to 30bar, 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. The dissociation and reassociation processes of amyloid protofibrils initiated by pressure-jump have been monitored with real-time super(1)H NMR spectroscopy using an intrinsically denatured disulfide-deficient variant of hen lysozyme. Upon pressure-jump up to 2kbar, the matured protofibrils grown over several months become fully dissociated into monomers within a few days. Upon pressure-jump down to 30bar, 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. lysozyme
Author	Tachibana, Hideki Kamatari, Yuji O. Yokoyama, Shigeyuki Akasaka, Kazuyuki
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Cites_doi	10.1046/j.1365-3083.1999.00508.x 10.1021/bi9904149 10.1016/S0022-2836(02)00425-4 10.1063/1.1334630 10.1016/S0021-9258(18)71557-3 10.1016/j.jmb.2004.02.067 10.1126/science.152.3730.1756 10.1016/S0167-4838(01)00346-6 10.1016/S0076-6879(02)38218-1 10.1074/jbc.274.36.25945 10.1016/S1074-5521(97)90303-3 10.1073/pnas.96.18.9989 10.1016/S0968-0004(99)01445-0 10.1073/pnas.1734009100 10.1016/S0014-5793(00)01904-9 10.1073/pnas.0305798101 10.1016/S0959-440X(98)80016-X
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Snippet	The dissociation and reassociation processes of amyloid protofibrils initiated by pressure-jump have been monitored with real-time 1H NMR spectroscopy using an... The dissociation and reassociation processes of amyloid protofibrils initiated by pressure-jump have been monitored with real-time (1)H NMR spectroscopy using... The dissociation and reassociation processes of amyloid protofibrils initiated by pressure-jump have been monitored with real-time super(1)H NMR spectroscopy...
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SubjectTerms	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
Title	Pressure-jump NMR Study of Dissociation and Association of Amyloid Protofibrils
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