| Pressure-accelerated dissociation of amyloid fibrils in wild-type hen lysozyme. | |
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MedLine Citation:
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PMID: 22225805 Owner: NLM Status: In-Data-Review |
Abstract/OtherAbstract:
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The dynamics of amyloid fibrils, including their formation and dissociation, could be of vital importance in life. We studied the kinetics of dissociation of the amyloid fibrils from wild-type hen lysozyme at 25°C in vitro as a function of pressure using Trp fluorescence as a probe. Upon 100-fold dilution of 8 mg ml(-1) fibril solution in 80 mM NaCl, pH 2.2, no immediate change occurred in Trp fluorescence, but at pressures of 50-450 MPa the fluorescence intensity decreased rapidly with time (k(obs) = 0.00193 min(-1) at 0.1 MPa, 0.0348 min(-1) at 400 MPa). This phenomenon is attributable to the pressure-accelerated dissociation of amyloid fibrils into monomeric hen lysozyme. From the pressure dependence of the rates, which reaches a plateau at ∼450 MPa, we determined the activation volume ΔV(0‡) = -32.9 ± 1.7 ml mol(monomer)(-1) and the activation compressibility Δκ(‡) = -0.0075 ± 0.0006 ml mol(monomer)(-1) bar(-1) for the dissociation reaction. The negative ΔV(0‡) and Δκ(‡) values are consistent with the notion that the amyloid fibril from wild-type hen lysozyme is in a high-volume and high-compressibility state, and the transition state for dissociation is coupled with a partial hydration of the fibril. |
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Authors:
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Buddha R Shah; Akihiro Maeno; Hiroshi Matsuo; Hideki Tachibana; Kazuyuki Akasaka |
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Publication Detail:
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Type: Journal Article Date: 2012-01-03 |
Journal Detail:
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Title: Biophysical journal Volume: 102 ISSN: 1542-0086 ISO Abbreviation: Biophys. J. Publication Date: 2012 Jan |
Date Detail:
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Created Date: 2012-01-09 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0370626 Medline TA: Biophys J Country: United States |
Other Details:
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Languages: eng Pagination: 121-6 Citation Subset: IM |
Copyright Information:
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Copyright © 2012 Biophysical Society. Published by Elsevier Inc. All rights reserved. |
Affiliation:
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High Pressure Protein Research Center, Institute of Advanced Technology, Kinki University, Kinokawa, Japan; Faculty of Science, Nepal Academy of Science and Technology, Kathmandu, Nepal. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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