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Solid-state NMR reveals differences in the packing arrangements of peptide aggregates derived from the aortic amyloid polypeptide medin

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Solid-state NMR reveals differences in the packing arrangements of peptide aggregates derived from the aortic amyloid polypeptide medin. / Davies, Hannah A; Madine, Jillian; Middleton, David A.
In: June 2002. ISSN 1460-4582, Vol. 18, No. 1, 01.2012, p. 65-72.

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Davies, Hannah A ; Madine, Jillian ; Middleton, David A. / Solid-state NMR reveals differences in the packing arrangements of peptide aggregates derived from the aortic amyloid polypeptide medin. In: June 2002. ISSN 1460-4582. 2012 ; Vol. 18, No. 1. pp. 65-72.

Bibtex

@article{133141c0bc3146a1bcb246b3930f62d9,
title = "Solid-state NMR reveals differences in the packing arrangements of peptide aggregates derived from the aortic amyloid polypeptide medin",
abstract = "Several polypeptides aggregate into insoluble amyloid fibrils associated with pathologies such as Alzheimer's disease, Parkinson's disease and type 2 diabetes. Understanding the structural and sequential motifs that drive fibrillisation may assist in the discovery and refinement of effective therapies. Here we investigate the effects of three predicted amyloidogenic regions on the structure of aggregates formed by medin, a poorly characterised polypeptide associated with aortic medial amyloidosis. Solid-state NMR is used to compare the dynamics and sheet packing arrangement of the C-terminal region encompassing residues F(43) GSV within full-length medin (Med(1-50) ) and two shorter peptide fragments, Med(30-50) and Med(42-49) , lacking specific sequences predicted to be amyloidogenic.(.) Results show that all three peptides have different aggregate morphologies, and Med(30-50) and Med(1-50) have different sheet packing arrangements and dynamics to Med(42-49) . These results imply that at least two of the three predicted amyloidogenic regions are required for the formation and elongation of medin fibres observed in the disease state.",
keywords = "Amino Acid Sequence, Amyloid, Amyloidosis, Antigens, Surface, Aorta, Biological Markers, Diabetes Mellitus, Type 2, Humans, Magnetic Resonance Spectroscopy, Microscopy, Electron, Milk Proteins, Molecular Sequence Data, Neurodegenerative Diseases, Peptide Fragments, Protein Structure, Secondary, Protein Structure, Tertiary, Spectrometry, Fluorescence, Thiazoles",
author = "Davies, {Hannah A} and Jillian Madine and Middleton, {David A}",
note = "Copyright {\textcopyright} 2011 European Peptide Society and John Wiley & Sons, Ltd.",
year = "2012",
month = jan,
doi = "10.1002/psc.1418",
language = "English",
volume = "18",
pages = "65--72",
journal = "June 2002. ISSN 1460-4582",
issn = "0893-3200",
publisher = "American Psychological Association Inc.",
number = "1",

}

RIS

TY - JOUR

T1 - Solid-state NMR reveals differences in the packing arrangements of peptide aggregates derived from the aortic amyloid polypeptide medin

AU - Davies, Hannah A

AU - Madine, Jillian

AU - Middleton, David A

N1 - Copyright © 2011 European Peptide Society and John Wiley & Sons, Ltd.

PY - 2012/1

Y1 - 2012/1

N2 - Several polypeptides aggregate into insoluble amyloid fibrils associated with pathologies such as Alzheimer's disease, Parkinson's disease and type 2 diabetes. Understanding the structural and sequential motifs that drive fibrillisation may assist in the discovery and refinement of effective therapies. Here we investigate the effects of three predicted amyloidogenic regions on the structure of aggregates formed by medin, a poorly characterised polypeptide associated with aortic medial amyloidosis. Solid-state NMR is used to compare the dynamics and sheet packing arrangement of the C-terminal region encompassing residues F(43) GSV within full-length medin (Med(1-50) ) and two shorter peptide fragments, Med(30-50) and Med(42-49) , lacking specific sequences predicted to be amyloidogenic.(.) Results show that all three peptides have different aggregate morphologies, and Med(30-50) and Med(1-50) have different sheet packing arrangements and dynamics to Med(42-49) . These results imply that at least two of the three predicted amyloidogenic regions are required for the formation and elongation of medin fibres observed in the disease state.

AB - Several polypeptides aggregate into insoluble amyloid fibrils associated with pathologies such as Alzheimer's disease, Parkinson's disease and type 2 diabetes. Understanding the structural and sequential motifs that drive fibrillisation may assist in the discovery and refinement of effective therapies. Here we investigate the effects of three predicted amyloidogenic regions on the structure of aggregates formed by medin, a poorly characterised polypeptide associated with aortic medial amyloidosis. Solid-state NMR is used to compare the dynamics and sheet packing arrangement of the C-terminal region encompassing residues F(43) GSV within full-length medin (Med(1-50) ) and two shorter peptide fragments, Med(30-50) and Med(42-49) , lacking specific sequences predicted to be amyloidogenic.(.) Results show that all three peptides have different aggregate morphologies, and Med(30-50) and Med(1-50) have different sheet packing arrangements and dynamics to Med(42-49) . These results imply that at least two of the three predicted amyloidogenic regions are required for the formation and elongation of medin fibres observed in the disease state.

KW - Amino Acid Sequence

KW - Amyloid

KW - Amyloidosis

KW - Antigens, Surface

KW - Aorta

KW - Biological Markers

KW - Diabetes Mellitus, Type 2

KW - Humans

KW - Magnetic Resonance Spectroscopy

KW - Microscopy, Electron

KW - Milk Proteins

KW - Molecular Sequence Data

KW - Neurodegenerative Diseases

KW - Peptide Fragments

KW - Protein Structure, Secondary

KW - Protein Structure, Tertiary

KW - Spectrometry, Fluorescence

KW - Thiazoles

U2 - 10.1002/psc.1418

DO - 10.1002/psc.1418

M3 - Journal article

C2 - 22102261

VL - 18

SP - 65

EP - 72

JO - June 2002. ISSN 1460-4582

JF - June 2002. ISSN 1460-4582

SN - 0893-3200

IS - 1

ER -