Sedimentation studies on human amylin fail to detect low-molecular-weight oligomers

Sara M. Vaiana; Rodolfo Ghirlando; Wai Ming Yau; William A. Eaton; James Hofrichter

doi:10.1529/biophysj.107.125146

Sedimentation studies on human amylin fail to detect low-molecular-weight oligomers

Sara M. Vaiana
, Rodolfo Ghirlando
, Wai Ming Yau
, William A. Eaton
, James Hofrichter

Research output: Contribution to journal › Article › peer-review

38 Scopus citations

Abstract

Sedimentation velocity experiments show that only monomers coexist with amyloid fibrils of human islet amyloidpolypeptide. No oligomers containing >100 monomers could be detected, suggesting that the putative toxic oligomers are much larger than those found for the Alzheimer's peptide, Aβ(1-42).

Original language	English (US)
Pages (from-to)	L45-L47
Journal	Biophysical journal
Volume	94
Issue number	7
DOIs	https://doi.org/10.1529/biophysj.107.125146
State	Published - Apr 2008
Externally published	Yes

ASJC Scopus subject areas

Biophysics

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10.1529/biophysj.107.125146

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title = "Sedimentation studies on human amylin fail to detect low-molecular-weight oligomers",

abstract = "Sedimentation velocity experiments show that only monomers coexist with amyloid fibrils of human islet amyloidpolypeptide. No oligomers containing >100 monomers could be detected, suggesting that the putative toxic oligomers are much larger than those found for the Alzheimer's peptide, Aβ(1-42).",

author = "Vaiana, \{Sara M.\} and Rodolfo Ghirlando and Yau, \{Wai Ming\} and Eaton, \{William A.\} and James Hofrichter",

note = "Funding Information: This work was supported by the Intramural Research Program of The National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health. ",

year = "2008",

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doi = "10.1529/biophysj.107.125146",

language = "English (US)",

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AU - Vaiana, Sara M.

AU - Ghirlando, Rodolfo

AU - Yau, Wai Ming

AU - Eaton, William A.

AU - Hofrichter, James

N1 - Funding Information: This work was supported by the Intramural Research Program of The National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health.

PY - 2008/4

Y1 - 2008/4

N2 - Sedimentation velocity experiments show that only monomers coexist with amyloid fibrils of human islet amyloidpolypeptide. No oligomers containing >100 monomers could be detected, suggesting that the putative toxic oligomers are much larger than those found for the Alzheimer's peptide, Aβ(1-42).

AB - Sedimentation velocity experiments show that only monomers coexist with amyloid fibrils of human islet amyloidpolypeptide. No oligomers containing >100 monomers could be detected, suggesting that the putative toxic oligomers are much larger than those found for the Alzheimer's peptide, Aβ(1-42).

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DO - 10.1529/biophysj.107.125146

M3 - Article

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AN - SCOPUS:41649117851

SN - 0006-3495

VL - 94

SP - L45-L47

JO - Biophysical journal

JF - Biophysical journal

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Sedimentation studies on human amylin fail to detect low-molecular-weight oligomers

Abstract

ASJC Scopus subject areas

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