High Pressure Bioscience and Biotechnology
Online ISSN : 1882-1723
ISSN-L : 1882-1723
Protein
Volume and Compressibility of Amyloid Fibrils
Hideki Tachibana, Kunihiko Gekko, Akihiro Nakamura, Koichi Matsuo, Abdul Raziq Abdul Latif, Mariko Araga, Ryouhei Kono, Kazuyuki Akasaka
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2008 Volume 2 Issue 1 Pages 15-23

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Abstract
Intrinsically unfolded hen lysozyme disulfide-deficient variant spontaneously forms amyloid-like fibrils. Its early assembly reversibly dissociates under high hydrostatic pressure with a partial molar volume decrease of 100 mL per monomeric unit. The partial specific volumes of the monomeric and protofibrillar states are 0.684 and 0.724 mL g-1, respectively, and the adiabatic compressibility coefficient of these states are -7.48 and 1.35 Mbar-1, which indicates that the protofibrillar state is highly voluminous and compressible. Pressure accelerates the dissociation of protofibrils with a negative activation volume of -50 ml mol-1 and a negative activation compressibility of -0.013 ml mol-1 bar-1, which suggests that partial hydration of existing voids takes place in the transition state of dissociation reaction.
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© 2008 Japanese Research Group of High Pressure Bioscience and Biotechnology
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