Mechanisms of ultrasonically induced fibrillation of amyloid β₁₋₄₀ peptides

Uesugi, Kentaro; Ogi, Hirotsugu; Fukushima, Masahiko; So, Masatomo; Yagi, Hisashi; Goto, Yuji; Hirao, Masahiko

doi:https://doi.org/10.7567/JJAP.52.07HE10

Mechanisms of ultrasonically induced fibrillation of amyloid β₁₋₄₀ peptides

Uesugi, Kentaro; Ogi, Hirotsugu; Fukushima, Masahiko et al.

Japanese Journal of Applied Physics, 2013, 52, 07HE10

Number of Access:528（2025-11-25 02:19 Counts）

Identifier to cite or link to this item: https://hdl.handle.net/11094/84169

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Title	Mechanisms of ultrasonically induced fibrillation of amyloid β₁₋₄₀ peptides
Creator	CreatorName Uesugi, Kentaro
	NRID 1000090252626 1000090252626 researchmap permalink read0042771 read0042771 Scopus Author ID 35563683500 35563683500 ORCID 0000-0002-9602-5194 0000-0002-9602-5194 CreatorName Ogi, Hirotsugu
	CreatorName Fukushima, Masahiko
	NRID 1000040746335 1000040746335 CreatorName So, Masatomo
	NRID 1000010432494 1000010432494 CreatorName Yagi, Hisashi
	NRID 1000040153770 1000040153770 researchmap permalink read0014440 read0014440 CreatorName Goto, Yuji
	NRID 1000080112027 1000080112027 CreatorName Hirao, Masahiko
Description	Kentaro Uesugi, Hirotsugu Ogi, Masahiko Fukushima, Masatomo So, Hisashi Yagi, Yuji Goto and Masahiko Hirao. Mechanisms of ultrasonically induced fibrillation of amyloid β₁₋₄₀ peptides. Japanese Journal of Applied Physics, 52(7S), 07HE10. https://doi.org/10.7567/JJAP.52.07HE10.
Abstract	We systematically study the relationship between the ultrasonically induced aggregation behavior of amyloid β₁₋₄₀ peptide and acoustic pressures to clarify the dominant mechanism of the aggregation. With ultrasonic irradiation, the thioflavin-T (ThT) level of the A solution rises after a lag time, takes a maximum at 5 h, and remains unchanged or decreases. Thus, we monitor the ThT level at 5 h to evaluate the progress of the β-sheet structure and investigate its correlation with the acoustic pressures of fundamental and harmonics waves. The second-harmonics-wave amplitude shows the highest correlation with the ThT level, indicating the dominant contribution of cavitation bubbles to the fibrillation phenomenon. The influence of solution pH and Ar gas are investigated to identify the aggregation mechanism. As a result, local condensation of the peptide due to the high affinity of hydrophobic residues to the bubble-solution interface causes a highly supersaturated solution, leading to precipitation of β-sheet-rich nuclei.
Publisher	The Japan Society of Applied Physics
Source Title	Japanese Journal of Applied Physics
Volume (Issue)	52
Page	07HE10
Date of Issued	2013-06-20
Language	English
Handle URL	https://hdl.handle.net/11094/84169
PISSN	00214922
eISSN	13474065
NCID	AA12295836
Relation.isVersionOf	DOI (Publisher Version) https://doi.org/10.7567/JJAP.52.07HE10
Access Rights	open access
oaire:version	Accepted Manuscript
Category	学術雑誌論文 Journal Article

Resource Type	journal article
Local Type	Journal Article
DCMI Type	Text
DCTERMS.bibliographicCitation	Japanese Journal of Applied Physics. 2013, 52, p. 07HE10
DC.title	Mechanisms of ultrasonically induced fibrillation of amyloid β₁₋₄₀ peptides
DC.creator	Uesugi, Kentaro
	Ogi, Hirotsugu
	Fukushima, Masahiko
	So, Masatomo
	Yagi, Hisashi
	Goto, Yuji
	Hirao, Masahiko
DC.publisher	The Japan Society of Applied Physics
DC.language' scheme='DCTERMS.RFC1766	English
DC.type' scheme='DCTERMS.DCMIType	Text
DCTERMS.issued' scheme='DCTERMS.W3CDTF	2013-06-20
DC.identifier	https://doi.org/10.7567/JJAP.52.07HE10
DC.description	Kentaro Uesugi, Hirotsugu Ogi, Masahiko Fukushima, Masatomo So, Hisashi Yagi, Yuji Goto and Masahiko Hirao. Mechanisms of ultrasonically induced fibrillation of amyloid β₁₋₄₀ peptides. Japanese Journal of Applied Physics, 52(7S), 07HE10. https://doi.org/10.7567/JJAP.52.07HE10.
DCTERMS.abstract	We systematically study the relationship between the ultrasonically induced aggregation behavior of amyloid β₁₋₄₀ peptide and acoustic pressures to clarify the dominant mechanism of the aggregation. With ultrasonic irradiation, the thioflavin-T (ThT) level of the A solution rises after a lag time, takes a maximum at 5 h, and remains unchanged or decreases. Thus, we monitor the ThT level at 5 h to evaluate the progress of the β-sheet structure and investigate its correlation with the acoustic pressures of fundamental and harmonics waves. The second-harmonics-wave amplitude shows the highest correlation with the ThT level, indicating the dominant contribution of cavitation bubbles to the fibrillation phenomenon. The influence of solution pH and Ar gas are investigated to identify the aggregation mechanism. As a result, local condensation of the peptide due to the high affinity of hydrophobic residues to the bubble-solution interface causes a highly supersaturated solution, leading to precipitation of β-sheet-rich nuclei.
DC.format	84169
citation_title	Mechanisms of ultrasonically induced fibrillation of amyloid β₁₋₄₀ peptides
citation_author	Uesugi, Kentaro
	Ogi, Hirotsugu
	Fukushima, Masahiko
	So, Masatomo
	Yagi, Hisashi
	Goto, Yuji
	Hirao, Masahiko
citation_publisher	The Japan Society of Applied Physics
citation_language	English
citation_date	2013-06-20
citation_journal_title	Japanese Journal of Applied Physics
citation_volume	52
citation_firstpage	07HE10
citation_doi	https://doi.org/10.7567/JJAP.52.07HE10
citation_public_url	https://hdl.handle.net/11094/84169

Mechanisms of ultrasonically induced fibrillation of amyloid β₁₋₄₀ peptides

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