A Comprehensive Model for Packing and Hydration for Amyloid Fibrils of β2-Microglobulin

Lee, Young-Ho; Chatani, Eri; Sasahara, Kenji; Naiki, Hironobu; Goto, Yuji

doi:https://doi.org/10.1074/jbc.M806939200

A Comprehensive Model for Packing and Hydration for Amyloid Fibrils of β2-Microglobulin

Lee, Young-Ho; Chatani, Eri; Sasahara, Kenji et al.

Journal of Biological Chemistry, 2009, 284(4), 2169-2175

Number of Access:681（2025-08-30 13:29 Counts）

Identifier to cite or link to this item: https://hdl.handle.net/11094/71287

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Title	A Comprehensive Model for Packing and Hydration for Amyloid Fibrils of β2-Microglobulin
Creator	NRID 1000070589431 1000070589431 CreatorName Lee, Young-Ho
	NRID 1000000432493 1000000432493 CreatorName Chatani, Eri
	NRID 1000020432495 1000020432495 CreatorName Sasahara, Kenji
	NRID 1000010227704 1000010227704 CreatorName Naiki, Hironobu
	NRID 1000040153770 1000040153770 researchmap permalink read0014440 read0014440 CreatorName Goto, Yuji
Description	This research was originally published in the Journal of Biological Chemistry. Young-Ho Lee, Eri Chatani, Kenji Sasahara, Hironobu Naiki and Yuji Goto. A Comprehensive Model for Packing and Hydration for Amyloid Fibrils of β2-Microglobulin. J. Biol. Chem. 2009; 284, 2169-2175. © the American Society for Biochemistry and Molecular Biology
Abstract	Volume can provide informative structural descriptions of macromolecules such as proteins in solution because a final volumetric outcome accompanies the exquisite equipoise of packing effects between residues, and residues and waters inside and outside proteins. Here we performed systematic investigations on the volumetric nature of the amyloidogenic conformations of β2-microglobulin (β2-m) and its amyloidogenic core peptide, K3, using a high precision densitometer. The transition from the acid-denatured β2-m to the mature amyloid fibrils was accompanied by a positive change in the partial specific volume, which was larger than that observed for the transition from the acid-denatured β2-m to the native structure. The data imply that the mature amyloid fibrils are more voluminous than the native structure because of a sparse packing density of side chains. In contrast, the formation of the mature amyloid-like fibrils of the K3 from the random coil was followed by a considerable decrease in the partial specific volume, suggesting a highly compact core structure. Interestingly, the immature amyloid-like fibrils of β2-m exhibited a volume intermediate between those of the mature fibrils of β2-m and K3, because of the core structure at their center and the relatively noncompact region around the core with much hydration. These volumetric differences would result from the nature of main-chain-dominated fibrillogenesis. We suggest comprehensive models for these three types of fibrils illustrating packing and hydrational states.
Publisher	American Society for Biochemistry and Molecular Biology
Source Title	Journal of Biological Chemistry
Volume (Issue)	284(4)
Page	2169-2175
Date of Issued	2009-01
Language	English
Handle URL	https://hdl.handle.net/11094/71287
eISSN	1083351X
NCID	AA1202456X
Relation.isIdenticalTo	DOI (Publisher Version) https://doi.org/10.1074/jbc.M806939200
Access Rights	open access
oaire:version	Version of Record
Category	学術雑誌論文 Journal Article

Resource Type	journal article
Local Type	Journal Article
DCMI Type	Text
DCTERMS.bibliographicCitation	Journal of Biological Chemistry. 2009, 284(4), p. 2169-2175
DC.title	A Comprehensive Model for Packing and Hydration for Amyloid Fibrils of β2-Microglobulin
DC.creator	Lee, Young-Ho
	Chatani, Eri
	Sasahara, Kenji
	Naiki, Hironobu
	Goto, Yuji
DC.publisher	American Society for Biochemistry and Molecular Biology
DC.language' scheme='DCTERMS.RFC1766	English
DC.type' scheme='DCTERMS.DCMIType	Text
DCTERMS.issued' scheme='DCTERMS.W3CDTF	2009-01
DC.identifier	https://doi.org/10.1074/jbc.M806939200
DC.description	This research was originally published in the Journal of Biological Chemistry. Young-Ho Lee, Eri Chatani, Kenji Sasahara, Hironobu Naiki and Yuji Goto. A Comprehensive Model for Packing and Hydration for Amyloid Fibrils of β2-Microglobulin. J. Biol. Chem. 2009; 284, 2169-2175. © the American Society for Biochemistry and Molecular Biology
DCTERMS.abstract	Volume can provide informative structural descriptions of macromolecules such as proteins in solution because a final volumetric outcome accompanies the exquisite equipoise of packing effects between residues, and residues and waters inside and outside proteins. Here we performed systematic investigations on the volumetric nature of the amyloidogenic conformations of β2-microglobulin (β2-m) and its amyloidogenic core peptide, K3, using a high precision densitometer. The transition from the acid-denatured β2-m to the mature amyloid fibrils was accompanied by a positive change in the partial specific volume, which was larger than that observed for the transition from the acid-denatured β2-m to the native structure. The data imply that the mature amyloid fibrils are more voluminous than the native structure because of a sparse packing density of side chains. In contrast, the formation of the mature amyloid-like fibrils of the K3 from the random coil was followed by a considerable decrease in the partial specific volume, suggesting a highly compact core structure. Interestingly, the immature amyloid-like fibrils of β2-m exhibited a volume intermediate between those of the mature fibrils of β2-m and K3, because of the core structure at their center and the relatively noncompact region around the core with much hydration. These volumetric differences would result from the nature of main-chain-dominated fibrillogenesis. We suggest comprehensive models for these three types of fibrils illustrating packing and hydrational states.
DC.format	71287
citation_title	A Comprehensive Model for Packing and Hydration for Amyloid Fibrils of β2-Microglobulin
citation_author	Lee, Young-Ho
	Chatani, Eri
	Sasahara, Kenji
	Naiki, Hironobu
	Goto, Yuji
citation_publisher	American Society for Biochemistry and Molecular Biology
citation_language	English
citation_date	2009-01
citation_journal_title	Journal of Biological Chemistry
citation_volume	284
citation_issue	4
citation_firstpage	2169
citation_lastpage	2175
citation_doi	https://doi.org/10.1074/jbc.M806939200
citation_public_url	https://hdl.handle.net/11094/71287

A Comprehensive Model for Packing and Hydration for Amyloid Fibrils of β2-Microglobulin

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