Characterizations of distinct amyloidogenic conformations of the Aβ (1–40) and (1–42) peptides

Kwang Hun Lim; Hilary H. Collver; Yen T.H. Le; Partha Nagchowdhuri; John M. Kenney

doi:10.1016/j.bbrc.2006.12.043

journal article Feb 01, 2007

Characterizations of distinct amyloidogenic conformations of the Aβ (1–40) and (1–42) peptides

Kwang Hun Lim Hilary H. Collver Yen T.H. Le Partha Nagchowdhuri John M. Kenney

Biochemical and Biophysical Research Communications Vol. 353 No. 2 pp. 443-449 · Elsevier BV

View at Publisher Save 10.1016/j.bbrc.2006.12.043

Topics

No keywords indexed for this article. Browse by subject →

References

33

[1]

Selkoe "The molecular pathology of Alzheimers-disease" Neuron (1991) 10.1016/0896-6273(91)90052-2

[2]

MODELS OF AMYLOID SEEDING IN ALZHEIMER'S DISEASE AND SCRAPIE: Mechanistic Truths and Physiological Consequences of the Time-Dependent Solubility of Amyloid Proteins

James D. Harper, Peter T. Lansbury

Annual Review of Biochemistry 1997 10.1146/annurev.biochem.66.1.385

[3]

Wood "Physical, morphological and functional differences between pH 5.8 and 7.4 aggregates of the Alzheimer’s amyloid peptide AP" J. Mol. Biol. (1996) 10.1006/jmbi.1996.0133

[4]

Wood "Selective inhibition of A beta fibril formation" J. Biol. Chem. (1996) 10.1074/jbc.271.8.4086

[5]

Kusumoto "Temperature dependence of amyloid beta-protein fibrillization" Proc. Natl. Acad. Sci. USA (1998) 10.1073/pnas.95.21.12277

[6]

Gursky "Temperature-dependent beta-sheet formation in beta-amyloid A beta(1–40) peptide in water: uncoupling beta-structure folding from aggregation" BBA-Protein Struct. Mol. Enzymol. (2000) 10.1016/s0167-4838(99)00228-9

[7]

Solution NMR Studies of the Aβ(1−40) and Aβ(1−42) Peptides Establish that the Met35 Oxidation State Affects the Mechanism of Amyloid Formation

Liming Hou, Haiyan Shao, Yongbo Zhang et al.

Journal of the American Chemical Society 2004 10.1021/ja036813f

[8]

Younkin "Evidence that a-beta-42 is the real culprit in Alzheimers-disease" Ann. Neurol. (1995) 10.1002/ana.410370303

[9]

Translating cell biology into therapeutic advances in Alzheimer's disease

Dennis J. Selkoe

Nature 1999 10.1038/399a023

[10]

Weggen "A subset of NSAIDs lower amyloidogenic A beta 42 independently of cyclooxygenase activity" Nature (2001) 10.1038/35102591

[11]

Dahlgren "Oligomeric and fibrillar species of amyloid-beta peptides differentially affect neuronal viability" J. Biol. Chem. (2002) 10.1074/jbc.m201750200

[12]

McGowan "A beta 42 is essential for parenchymal and vascular amyloid deposition in mice" Neuron (2005) 10.1016/j.neuron.2005.06.030

[13]

Amyloid β-protein (Aβ) assembly: Aβ40 and Aβ42 oligomerize through distinct pathways

Gal Bitan, Marina D. Kirkitadze, Aleksey Lomakin et al.

Proceedings of the National Academy of Sciences 2003 10.1073/pnas.222681699

[14]

Urbanc "In silico study of amyloid beta-protein folding and oligomerization" Proc. Natl. Acad. Sci. USA (2004) 10.1073/pnas.0408153101

[15]

Distinct Early Folding and Aggregation Properties of Alzheimer Amyloid-β Peptides Aβ40 and Aβ42

Yun-Ru Chen, Charles G. Glabe

Journal of Biological Chemistry 2006 10.1074/jbc.m602363200

[16]

Teplow "Elucidating amyloid beta-protein folding and assembly: A multidisciplinary approach" Acc. Chem. Res. (2006) 10.1021/ar050063s

[17]

Conformational constraints for amyloid fibrillation: the importance of being unfolded

Vladimir N. Uversky, Anthony L. Fink

Biochimica et Biophysica Acta (BBA) - Proteins and... 2004 10.1016/j.bbapap.2003.12.008

[18]

Protein folding and misfolding

Christopher M. Dobson

Nature 2003 10.1038/nature02261

[19]

Kelly "The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways" Curr. Opin. Struct. Biol. (1998) 10.1016/s0959-440x(98)80016-x

[20]

Amyloid β-Protein Fibrillogenesis

Dominic M. Walsh, Dean M. Hartley, Yoko Kusumoto et al.

Journal of Biological Chemistry 1999 10.1074/jbc.274.36.25945

[21]

Identification and characterization of key kinetic intermediates in amyloid β-protein fibrillogenesis11Edited by F. Cohen

Marina D Kirkitadze, Margaret M Condron, David B Teplow

Journal of Molecular Biology 2001 10.1006/jmbi.2001.4970

[22]

Barrow "Solution structures of beta peptide and its constituent fragments—relation to amyloid deposition" Science (1991) 10.1126/science.1853202

[23]

The Alzheimer's Peptide Aβ Adopts a Collapsed Coil Structure in Water

S. Zhang, K. Iwata, M.J. Lachenmann et al.

Journal of Structural Biology 2000 10.1006/jsbi.2000.4288

[24]

On the nucleation of amyloid β‐protein monomer folding

Noel D. Lazo, Marianne A. Grant, Margaret C. Condron et al.

Protein Science 2005 10.1110/ps.041292205

[25]

Jarvet "A left-handed 3(1) helical conformation in the Alzheimer A beta(12–28) peptide" FEBS Lett. (2003) 10.1016/s0014-5793(03)01293-6

[26]

Riek "NMR studies in aqueous solution fail to identify significant conformational differences between the monomeric forms of two Alzheimer peptides with widely different plaque-competence, A beta(1–40)(ox) and A beta(1–42)(ox)" Eur. J. Biochem. (2001) 10.1046/j.0014-2956.2001.02537.x

[27]

Lim "A Weakly Clustered N-terminus Inhibits Ab Amyloidogenesis" ChemBioChem (2006) 10.1002/cbic.200600270

[28]

Stine "In vitro characterization of conditions for amyloid-beta peptide oligomerization and fibrillogenesis" J. Biol. Chem. (2003) 10.1074/jbc.m210207200

[29]

Hou "Methionine 35 oxidation reduces fibril assembly of the amyloid A beta-(1–42) peptide of Alzheimer’s disease" J. Biol. Chem. (2002) 10.1074/jbc.c200338200

[30]

Jarvet "Reversible random coil to beta-sheet transition and the early stage of aggregation of the A beta(12–28) fragment from the Alzheimer peptide" J. Am. Chem. Soc. (2000) 10.1021/ja991167z

[31]

Soreghan "Surfactant properties of Alzheimers a-beta peptides and the mechanism of amyloid aggregation" J. Biol. Chem. (1994) 10.1016/s0021-9258(19)61939-3

[32]

Relationship between nuclear magnetic resonance chemical shift and protein secondary structure

D.S. Wishart, B.D. Sykes, F.M. Richards

Journal of Molecular Biology 1991 10.1016/0022-2836(91)90214-q

[33]

Wolfe "Therapeutic strategies for Alzheimer’s disease" Nat. Rev. Drug Discov. (2002) 10.1038/nrd938

Cited By

72

Diffusion tensor image analysis along the perivascular space index alterations in Alzheimer’s disease: associated with cerebrospinal fluid Aβ40 and cognition

Junling Han, Yanlai Xia · 2026

Brain Imaging and Behavior

Effects of Ions and Small Compounds on the Structure of Aβ42 Monomers

Farbod Mahmoudinobar, Bradley L. Nilsson · 2021

The Journal of Physical Chemistry B

Differences in β-strand Populations of Monomeric Aβ40 and Aβ42

K. Aurelia Ball, Aaron H. Phillips · 2013

Biophysical Journal

Distinct Dimerization for Various Alloforms of the Amyloid-Beta Protein: Aβ1–40, Aβ1–42, and Aβ1–40(D23N)

Sébastien Coté, Rozita Laghaei · 2012

The Journal of Physical Chemistry B

The Structures of the E22Δ Mutant-Type Amyloid-β Alloforms and the Impact of E22Δ Mutation on the Structures of the Wild-Type Amyloid-β Alloforms

Orkid Coskuner, Olivia Wise-Scira · 2012

ACS Chemical Neuroscience

A partially folded structure of amyloid-beta(1–40) in an aqueous environment

Subramanian Vivekanandan, Jeffrey R. Brender · 2011

Biochemical and Biophysical Researc...

Distinct Morphologies for Amyloid Beta Protein Monomer: Aβ1–40, Aβ1–42, and Aβ1–40(D23N)

Sébastien Coté, Philippe Derreumaux · 2011

Journal of Chemical Theory and Comp...

Elucidation of Amyloid β-Protein Oligomerization Mechanisms: Discrete Molecular Dynamics Study

B. Urbanc, M. Betnel · 2010

Journal of the American Chemical So...

Amyloid β-Protein Monomer Folding: Free-Energy Surfaces Reveal Alloform-Specific Differences

Mingfeng Yang, David B. Teplow · 2008

Journal of Molecular Biology

Methyl dynamics of the amyloid-β peptides Aβ40 and Aβ42

Yilin Yan, Jiajing Liu · 2007

Biochemical and Biophysical Researc...

Metrics

72

Citations

33

References

Details

Published: Feb 01, 2007
Vol/Issue: 353(2)
Pages: 443-449
License: View

Authors

Funding

National Institutes of Health Award: P41GM66326

National Science Foundation Award: BIR-9214394

Cite This Article

Kwang Hun Lim, Hilary H. Collver, Yen T.H. Le, et al. (2007). Characterizations of distinct amyloidogenic conformations of the Aβ (1–40) and (1–42) peptides. Biochemical and Biophysical Research Communications, 353(2), 443-449. https://doi.org/10.1016/j.bbrc.2006.12.043

Characterizations of distinct amyloidogenic conformations of the Aβ (1–40) and (1–42) peptides

You May Also Like