Characterizations of distinct amyloidogenic conformations of the Abeta (1-40) and (1-42) peptides.

Characterizations of distinct amyloidogenic conformations of the Abeta (1-40) and (1-42) peptides. Research Abstract Details 

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Characterizations of distinct amyloidogenic conformations of the Abeta (1-40) and (1-42) peptides. Abstract Text:

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

Major constituents of the amyloid plaques found in the brain of Alzheimer's patients are the 39-43 residue beta-amyloid (Abeta) peptides. Extensive in vitro as well as in vivo biochemical studies have shown that the 40- and 42-residue Abeta peptides play major roles in the neurodegenerative pathology of Alzheimer's disease. Although the two Abeta peptides share common aggregation properties, the 42-residue peptide is more amyloidogenic and more strongly associated with amyloid pathology. Thus, characterizations of the two Abeta peptides are of critical importance in understanding the molecular mechanism of Abeta amyloid formation. In this report, we present combined CD and NMR studies of the monomeric states of the two peptides under both non-amyloidogenic (<5 degrees C) and amyloid-forming conditions (>5 degrees C) at physiological pH. Our CD studies of the Abeta peptides showed that initially unfolded Abeta peptides at low temperature (<5 degrees C) gradually underwent conformational changes to more beta-sheet-like monomeric intermediate states at stronger amyloidogenic conditions (higher temperatures). Detailed residue-specific information on the structural transition was obtained by using NMR spectroscopy. Residues in the N-terminal (3-12) and 20-22 regions underwent conformational changes to more extended structures at the stronger amyloidogenic conditions. Almost identical structural transitions of those residues were observed in the two Abeta peptides, suggesting a similar amyloidogenic intermediate for the two peptides. The 42-residue Abeta (1-42) peptide was, however, more significantly structured at the C-terminal region (39-42), which may lead to the different aggregation propensity of the two peptides.

Characterizations of distinct amyloidogenic conformations of the Abeta (1-40) and (1-42) peptides. Publishing Authors By Initials

KH Lim,HH Collver,YT Le,P Nagchowdhuri,JM Kenney,

For similar environment and public health: environment: environment, controlled: temperature research abstracts see: environment and public health: environment: environment, controlled: temperature research

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Characterizations of distinct amyloidogenic conformations of the Abeta (1-40) and (1-42) peptides. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: Biochemical and biophysical research communication

VOLUME: 353

Page Numbers: 443-9

Journal Abbreviation: Biochem. Biophys. Res. Commun.

ISSN: 0006-291X

DAY: 15

MONTH: 12

YEAR: 2006

Characterizations of distinct amyloidogenic conformations of the Abeta (1-40) and (1-42) peptides. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 372516

Characterizations of distinct amyloidogenic conformations of the Abeta (1-40) and (1-42) peptides. Keywords Mesh Terms:

KEYWORDS: Temperature

MESH TERMS: ultrastructure

Chemical & Substance for Abstract: Characterizations of distinct amyloidogenic conformations of the Abeta (1-40) and (1-42) peptides. Information

Substance Name: amyloid beta-protein (1-42)

Registry Number: 0

Grant and Affiliation Information for Characterizations of distinct amyloidogenic conformations of the Abeta (1-40) and (1-42) peptides.

AFFILIATION: Department of Chemistry, East Carolina University, Greenville, NC 27858, USA. limk@ecu.edu

Country: United States

AGENCY: United States NCRR

GRANT: P41RR02301

ACRONYM: RR

MEDLINETA: Biochem Biophys Res Commun

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