Energy landscape of polymorphic amyloid generation of β2-microglobulin revealed by calorimetry

Misaki Kinoshita; Yuxi Lin; Itoh Dai; Masaki Okumura; Natalia Markova; John E. Ladbury; Fabio Sterpone; Young Ho Lee

doi:10.1039/c8cc02718h

Energy landscape of polymorphic amyloid generation of β2-microglobulin revealed by calorimetry

Misaki Kinoshita, Yuxi Lin, Itoh Dai, Masaki Okumura, Natalia Markova, John E. Ladbury, Fabio Sterpone, Young Ho Lee

FRIS - Creative Interdisciplinary Research Division

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13 Citations (Scopus)

Abstract

Understanding of amyloid aggregation in terms of thermodynamics and kinetics is still limited. We herein examined the mechanism of β2-microglobulin amyloidogenesis using our unique method of isothermal titration calorimetry-based thermodynamic/kinetic measurements, and revealed the energy landscape of polymorphic amyloidogenesis under biological environment-mimicking conditions including shear forces and crowding effects.

Original language	English
Pages (from-to)	7995-7998
Number of pages	4
Journal	Chemical Communications
Volume	54
Issue number	57
DOIs	https://doi.org/10.1039/c8cc02718h
Publication status	Published - 2018

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abstract = "Understanding of amyloid aggregation in terms of thermodynamics and kinetics is still limited. We herein examined the mechanism of β2-microglobulin amyloidogenesis using our unique method of isothermal titration calorimetry-based thermodynamic/kinetic measurements, and revealed the energy landscape of polymorphic amyloidogenesis under biological environment-mimicking conditions including shear forces and crowding effects.",

author = "Misaki Kinoshita and Yuxi Lin and Itoh Dai and Masaki Okumura and Natalia Markova and Ladbury, {John E.} and Fabio Sterpone and Lee, {Young Ho}",

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AU - Kinoshita, Misaki

AU - Lin, Yuxi

AU - Dai, Itoh

AU - Okumura, Masaki

AU - Markova, Natalia

AU - Ladbury, John E.

AU - Sterpone, Fabio

AU - Lee, Young Ho

PY - 2018

Y1 - 2018

N2 - Understanding of amyloid aggregation in terms of thermodynamics and kinetics is still limited. We herein examined the mechanism of β2-microglobulin amyloidogenesis using our unique method of isothermal titration calorimetry-based thermodynamic/kinetic measurements, and revealed the energy landscape of polymorphic amyloidogenesis under biological environment-mimicking conditions including shear forces and crowding effects.

AB - Understanding of amyloid aggregation in terms of thermodynamics and kinetics is still limited. We herein examined the mechanism of β2-microglobulin amyloidogenesis using our unique method of isothermal titration calorimetry-based thermodynamic/kinetic measurements, and revealed the energy landscape of polymorphic amyloidogenesis under biological environment-mimicking conditions including shear forces and crowding effects.

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JO - Chemical Communications

JF - Chemical Communications

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ER -

Energy landscape of polymorphic amyloid generation of β2-microglobulin revealed by calorimetry

Abstract

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