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Development of a proteolytically stable retro-inverso peptide inhibitor of β-amyloid oligomerization as a potential novel treatment for Alzheimer's disease

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Development of a proteolytically stable retro-inverso peptide inhibitor of β-amyloid oligomerization as a potential novel treatment for Alzheimer's disease. / Taylor, Mark; Moore, Susan; Mayes, Jennifer; Parkin, Edward; Beeg, Marten; Canovi, Mara; Gobbi, Marco; Mann, David M A; Allsop, David.

In: Biochemistry, Vol. 49, No. 15, 2010, p. 3261-3272.

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Taylor, Mark ; Moore, Susan ; Mayes, Jennifer ; Parkin, Edward ; Beeg, Marten ; Canovi, Mara ; Gobbi, Marco ; Mann, David M A ; Allsop, David. / Development of a proteolytically stable retro-inverso peptide inhibitor of β-amyloid oligomerization as a potential novel treatment for Alzheimer's disease. In: Biochemistry. 2010 ; Vol. 49, No. 15. pp. 3261-3272.

Bibtex

@article{004d2b6b9fe743be92061e7db6d4e6eb,
title = "Development of a proteolytically stable retro-inverso peptide inhibitor of β-amyloid oligomerization as a potential novel treatment for Alzheimer's disease",
abstract = "The formation of beta-amyloid (Abeta) deposits in the brain is likely to be a seminal step in the development of Alzheimer's disease. Recent studies support the hypothesis that Abeta soluble oligomers are toxic to cells and have potent effects on memory and learning. Inhibiting the early stages of Abeta aggregation could, therefore, provide a novel approach to treating the underlying cause of AD. We have designed a retro-inverso peptide (RI-OR2, H(2)N-r",
keywords = "Alzheimer Disease, Amino Acid Sequence, Amyloid beta-Peptides, Animals, Cell Aggregation, Cell Line, Cell Survival, Humans, Immunoassay, Molecular Sequence Data, Peptide Fragments, Peptides, Surface Plasmon Resonance, Thiazoles",
author = "Mark Taylor and Susan Moore and Jennifer Mayes and Edward Parkin and Marten Beeg and Mara Canovi and Marco Gobbi and Mann, {David M A} and David Allsop",
year = "2010",
doi = "10.1021/bi100144m",
language = "English",
volume = "49",
pages = "3261--3272",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "American Chemical Society",
number = "15",

}

RIS

TY - JOUR

T1 - Development of a proteolytically stable retro-inverso peptide inhibitor of β-amyloid oligomerization as a potential novel treatment for Alzheimer's disease

AU - Taylor, Mark

AU - Moore, Susan

AU - Mayes, Jennifer

AU - Parkin, Edward

AU - Beeg, Marten

AU - Canovi, Mara

AU - Gobbi, Marco

AU - Mann, David M A

AU - Allsop, David

PY - 2010

Y1 - 2010

N2 - The formation of beta-amyloid (Abeta) deposits in the brain is likely to be a seminal step in the development of Alzheimer's disease. Recent studies support the hypothesis that Abeta soluble oligomers are toxic to cells and have potent effects on memory and learning. Inhibiting the early stages of Abeta aggregation could, therefore, provide a novel approach to treating the underlying cause of AD. We have designed a retro-inverso peptide (RI-OR2, H(2)N-r

AB - The formation of beta-amyloid (Abeta) deposits in the brain is likely to be a seminal step in the development of Alzheimer's disease. Recent studies support the hypothesis that Abeta soluble oligomers are toxic to cells and have potent effects on memory and learning. Inhibiting the early stages of Abeta aggregation could, therefore, provide a novel approach to treating the underlying cause of AD. We have designed a retro-inverso peptide (RI-OR2, H(2)N-r

KW - Alzheimer Disease

KW - Amino Acid Sequence

KW - Amyloid beta-Peptides

KW - Animals

KW - Cell Aggregation

KW - Cell Line

KW - Cell Survival

KW - Humans

KW - Immunoassay

KW - Molecular Sequence Data

KW - Peptide Fragments

KW - Peptides

KW - Surface Plasmon Resonance

KW - Thiazoles

U2 - 10.1021/bi100144m

DO - 10.1021/bi100144m

M3 - Journal article

C2 - 20230062

VL - 49

SP - 3261

EP - 3272

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

IS - 15

ER -