Kinetic Analysis of Amyloid Protofibril Dissociation and Volumetric Properties of the Transition State

We present here the first detailed kinetic analysis of the dissociation reaction of amyloid protofibrils by utilizing pressure as an accelerator of the reaction. The experiment is carried out on an excessively diluted typical protofibril solution formed from an intrinsically denatured disulfide-defi...

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Vydáno v:	Biophysical journal Ročník 92; číslo 1; s. 323 - 329
Hlavní autoři:	Abdul Latif, Abdul Raziq, Kono, Ryohei, Tachibana, Hideki, Akasaka, Kazuyuki
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	United States Elsevier Inc 01.01.2007 Biophysical Society
Témata:	Amyloid beta-Peptides - chemistry Animals Biophysics - methods Cell Biophysics Chickens Disulfides - chemistry Fibers Fluorescence Hydration Kinetics Microscopy, Atomic Force Microscopy, Fluorescence Molecules Muramidase - chemistry Peptide Fragments Pressure Protein Denaturation Proteins Thermodynamics Time Factors
ISSN:	0006-3495, 1542-0086
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Abstract	We present here the first detailed kinetic analysis of the dissociation reaction of amyloid protofibrils by utilizing pressure as an accelerator of the reaction. The experiment is carried out on an excessively diluted typical protofibril solution formed from an intrinsically denatured disulfide-deficient variant of hen lysozyme with Trp fluorescence as the reporter in the pressure range 3–400 MPa. From the analysis of the time-dependent fluorescence decay and the length distribution of the protofibrils measured on atomic force microscopy, we conclude that the protofibril grows or decays by attachment or detachment of a monomer at one end of the protofibril with a monomer dissociation rate independent of the length of the fibril. Furthermore, we find that the dissociation reaction is strongly dependent on pressure, characterized with a negative activation volume Δ V o‡ = −50.5 ± 1.60 ml mol −1 at 0.1 MPa and with a negative activation compressibility Δ κ ‡ = −0.013 ± 0.001 ml mol −1 bar −1 or −0.9 × 10 −6 ml g −1 bar −1. These results indicate that the protofibril is a highly compressible high-volume state, but that it becomes less compressible and less voluminous in the transition state, most probably due to partial hydration of the existing voids. The system eventually reaches the lowest-volume state with full hydration of the monomer in the dissociated state.
AbstractList	We present here the first detailed kinetic analysis of the dissociation reaction of amyloid protofibrils by utilizing pressure as an accelerator of the reaction. The experiment is carried out on an excessively diluted typical protofibril solution formed from an intrinsically denatured disulfide-deficient variant of hen lysozyme with Trp fluorescence as the reporter in the pressure range 3-400 MPa. From the analysis of the time-dependent fluorescence decay and the length distribution of the protofibrils measured on atomic force microscopy, we conclude that the protofibril grows or decays by attachment or detachment of a monomer at one end of the protofibril with a monomer dissociation rate independent of the length of the fibril. Furthermore, we find that the dissociation reaction is strongly dependent on pressure, characterized with a negative activation volume DeltaV(odouble dagger) = -50.5 +/- 1.60 ml mol(-1) at 0.1 MPa and with a negative activation compressibility Deltakappa(double dagger) = -0.013 +/- 0.001 ml mol(-1) bar(-1) or -0.9 x 10(-6) ml g(-1) bar(-1). These results indicate that the protofibril is a highly compressible high-volume state, but that it becomes less compressible and less voluminous in the transition state, most probably due to partial hydration of the existing voids. The system eventually reaches the lowest-volume state with full hydration of the monomer in the dissociated state.We present here the first detailed kinetic analysis of the dissociation reaction of amyloid protofibrils by utilizing pressure as an accelerator of the reaction. The experiment is carried out on an excessively diluted typical protofibril solution formed from an intrinsically denatured disulfide-deficient variant of hen lysozyme with Trp fluorescence as the reporter in the pressure range 3-400 MPa. From the analysis of the time-dependent fluorescence decay and the length distribution of the protofibrils measured on atomic force microscopy, we conclude that the protofibril grows or decays by attachment or detachment of a monomer at one end of the protofibril with a monomer dissociation rate independent of the length of the fibril. Furthermore, we find that the dissociation reaction is strongly dependent on pressure, characterized with a negative activation volume DeltaV(odouble dagger) = -50.5 +/- 1.60 ml mol(-1) at 0.1 MPa and with a negative activation compressibility Deltakappa(double dagger) = -0.013 +/- 0.001 ml mol(-1) bar(-1) or -0.9 x 10(-6) ml g(-1) bar(-1). These results indicate that the protofibril is a highly compressible high-volume state, but that it becomes less compressible and less voluminous in the transition state, most probably due to partial hydration of the existing voids. The system eventually reaches the lowest-volume state with full hydration of the monomer in the dissociated state. We present here the first detailed kinetic analysis of the dissociation reaction of amyloid protofibrils by utilizing pressure as an accelerator of the reaction. The experiment is carried out on an excessively diluted typical protofibril solution formed from an intrinsically denatured disulfide-deficient variant of hen lysozyme with Trp fluorescence as the reporter in the pressure range 3-400 MPa. From the analysis of the time-dependent fluorescence decay and the length distribution of the protofibrils measured on atomic force microscopy, we conclude that the protofibril grows or decays by attachment or detachment of a monomer at one end of the protofibril with a monomer dissociation rate independent of the length of the fibril. Furthermore, we find that the dissociation reaction is strongly dependent on pressure, characterized with a negative activation volume DeltaV(odouble dagger) = -50.5 +/- 1.60 ml mol(-1) at 0.1 MPa and with a negative activation compressibility Deltakappa(double dagger) = -0.013 +/- 0.001 ml mol(-1) bar(-1) or -0.9 x 10(-6) ml g(-1) bar(-1). These results indicate that the protofibril is a highly compressible high-volume state, but that it becomes less compressible and less voluminous in the transition state, most probably due to partial hydration of the existing voids. The system eventually reaches the lowest-volume state with full hydration of the monomer in the dissociated state. We present here the first detailed kinetic analysis of the dissociation reaction of amyloid protofibrils by utilizing pressure as an accelerator of the reaction. The experiment is carried out on an excessively diluted typical protofibril solution formed from an intrinsically denatured disulfide-deficient variant of hen lysozyme with Trp fluorescence as the reporter in the pressure range 3–400 MPa. From the analysis of the time-dependent fluorescence decay and the length distribution of the protofibrils measured on atomic force microscopy, we conclude that the protofibril grows or decays by attachment or detachment of a monomer at one end of the protofibril with a monomer dissociation rate independent of the length of the fibril. Furthermore, we find that the dissociation reaction is strongly dependent on pressure, characterized with a negative activation volume ΔVo‡ = −50.5 ± 1.60 ml mol−1 at 0.1 MPa and with a negative activation compressibility Δκ‡ = −0.013 ± 0.001 ml mol−1 bar−1 or −0.9 × 10−6 ml g−1 bar−1. These results indicate that the protofibril is a highly compressible high-volume state, but that it becomes less compressible and less voluminous in the transition state, most probably due to partial hydration of the existing voids. The system eventually reaches the lowest-volume state with full hydration of the monomer in the dissociated state. We present here the first detailed kinetic analysis of the dissociation reaction of amyloid protofibrils by utilizing pressure as an accelerator of the reaction. The experiment is carried out on an excessively diluted typical protofibril solution formed from an intrinsically denatured disulfide-deticient variant of hen lysozyme with Trp fluorescence as the reporter in the pressure range 3-400 MPa. From the analysis of the time-dependent fluorescence decay and the length distribution of the protofibrils measured on atomic force microscopy, we conclude that the protofibril grows or decays by attachment or detachment of a monomer at one end of the protofibril with a monomer dissociation rate independent of the length of the fibril. Furthermore, we find that the dissociation reaction is strongly dependent on pressure, characterized with a negative activation volume ΔV^sup o^[double dagger] = -50.5 ± 1.60 ml mol^sup -1^ at 0.1 MPa and with a negative activation compressibility Δκ[double dagger] = -0.013 ± 0.001 ml mol^sup -1^ bar^sup -1^ or -0.9 × 10^sup -6^ ml g^sup -1^ bar^sup -1^. These results indicate that the protofibril is a highly compressible high-volume state, but that it becomes less compressible and less voluminous in the transition state, most probably due to partial hydration of the existing voids. The system eventually reaches the lowest-volume state with full hydration of the monomer in the dissociated state. [PUBLICATION ABSTRACT] We present here the first detailed kinetic analysis of the dissociation reaction of amyloid protofibrils by utilizing pressure as an accelerator of the reaction. The experiment is carried out on an excessively diluted typical protofibril solution formed from an intrinsically denatured disulfide-deficient variant of hen lysozyme with Trp fluorescence as the reporter in the pressure range 3–400 MPa. From the analysis of the time-dependent fluorescence decay and the length distribution of the protofibrils measured on atomic force microscopy, we conclude that the protofibril grows or decays by attachment or detachment of a monomer at one end of the protofibril with a monomer dissociation rate independent of the length of the fibril. Furthermore, we find that the dissociation reaction is strongly dependent on pressure, characterized with a negative activation volume Δ V o‡ = −50.5 ± 1.60 ml mol −1 at 0.1 MPa and with a negative activation compressibility Δ κ ‡ = −0.013 ± 0.001 ml mol −1 bar −1 or −0.9 × 10 −6 ml g −1 bar −1. These results indicate that the protofibril is a highly compressible high-volume state, but that it becomes less compressible and less voluminous in the transition state, most probably due to partial hydration of the existing voids. The system eventually reaches the lowest-volume state with full hydration of the monomer in the dissociated state.
Author	Kono, Ryohei Tachibana, Hideki Abdul Latif, Abdul Raziq Akasaka, Kazuyuki
AuthorAffiliation	Department of Biotechnological Science, School of Biology-Oriented Science and Technology, Kinki University, Wakayama, Japan; and † Department of Biology, Faculty of Science, Kobe University, Kobe, Japan
AuthorAffiliation_xml	– name: Department of Biotechnological Science, School of Biology-Oriented Science and Technology, Kinki University, Wakayama, Japan; and † Department of Biology, Faculty of Science, Kobe University, Kobe, Japan
Author_xml	– sequence: 1 givenname: Abdul Raziq surname: Abdul Latif fullname: Abdul Latif, Abdul Raziq organization: Department of Biotechnological Science, School of Biology-Oriented Science and Technology, Kinki University, Wakayama, Japan; and – sequence: 2 givenname: Ryohei surname: Kono fullname: Kono, Ryohei organization: Department of Biotechnological Science, School of Biology-Oriented Science and Technology, Kinki University, Wakayama, Japan; and – sequence: 3 givenname: Hideki surname: Tachibana fullname: Tachibana, Hideki organization: Department of Biology, Faculty of Science, Kobe University, Kobe, Japan – sequence: 4 givenname: Kazuyuki surname: Akasaka fullname: Akasaka, Kazuyuki email: akasaka8@spring8.or.jp organization: Department of Biotechnological Science, School of Biology-Oriented Science and Technology, Kinki University, Wakayama, Japan; and
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CitedBy_id	crossref_primary_10_1016_j_bpj_2011_10_041 crossref_primary_10_1080_08957959_2010_530266 crossref_primary_10_1111_1541_4337_12462 crossref_primary_10_1016_j_abb_2012_11_016 crossref_primary_10_1074_jbc_M110_192872 crossref_primary_10_1002_cphc_202000074 crossref_primary_10_1039_D1SC06782F crossref_primary_10_1039_C3CC45844J crossref_primary_10_1529_biophysj_107_123000 crossref_primary_10_1002_elps_201400468 crossref_primary_10_3390_e12061632
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Copyright	2007 The Biophysical Society Copyright Biophysical Society Jan 1, 2007 Copyright © 2007, Biophysical Society 2007
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Snippet	We present here the first detailed kinetic analysis of the dissociation reaction of amyloid protofibrils by utilizing pressure as an accelerator of the...
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SubjectTerms	Amyloid beta-Peptides - chemistry Animals Biophysics - methods Cell Biophysics Chickens Disulfides - chemistry Fibers Fluorescence Hydration Kinetics Microscopy, Atomic Force Microscopy, Fluorescence Molecules Muramidase - chemistry Peptide Fragments Pressure Protein Denaturation Proteins Thermodynamics Time Factors
Title	Kinetic Analysis of Amyloid Protofibril Dissociation and Volumetric Properties of the Transition State
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