Transient formation of nano-crystalline structures during fibrillation of an Aβ-like peptide

Daniel E. Otzen; Mikael Oliveberg

doi:10.1110/ps.03538904

Transient formation of nano-crystalline structures during fibrillation of an Aβ-like peptide

^*Corresponding author for this work

Interdisciplinary Nanoscience Center - INANO-MBG, iNANO-huset

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

12 Citations (Scopus)

Abstract

During the first few minutes of fibrillation of a 14-residue peptide homologous to the hydrophobic C-terminal part of the Aβ-peptide, EM micrographs reveal small crystalline areas (100 to 150 nm, repeating unit 47 Å) scattered in more amorphous material. On a longer time scale, these crystalline areas disappear and are replaced by tangled clusters resembling protofilaments (hours), and eventually by more regular amyloid fibrils of 60 Å to 120 Å diameter (days). The transient population of the crystalline areas indicates the presence of ordered substructures in the early fibrillation process, the diameter of which matches the length of the 14-mer peptide in an extended β-strand conformation.

Original language	English
Journal	Protein Science
Volume	13
Issue	5
Pages (from-to)	1417-1421
Number of pages	5
ISSN	0961-8368
DOIs	https://doi.org/10.1110/ps.03538904
Publication status	Published - 1 May 2004

Keywords

Amyloid fibrils
Electron microscopy
Peptide aggregation
Peptide crystal
Protein aggregation

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title = "Transient formation of nano-crystalline structures during fibrillation of an Aβ-like peptide",

abstract = "During the first few minutes of fibrillation of a 14-residue peptide homologous to the hydrophobic C-terminal part of the Aβ-peptide, EM micrographs reveal small crystalline areas (100 to 150 nm, repeating unit 47 {\AA}) scattered in more amorphous material. On a longer time scale, these crystalline areas disappear and are replaced by tangled clusters resembling protofilaments (hours), and eventually by more regular amyloid fibrils of 60 {\AA} to 120 {\AA} diameter (days). The transient population of the crystalline areas indicates the presence of ordered substructures in the early fibrillation process, the diameter of which matches the length of the 14-mer peptide in an extended β-strand conformation.",

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AU - Otzen, Daniel E.

AU - Oliveberg, Mikael

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N2 - During the first few minutes of fibrillation of a 14-residue peptide homologous to the hydrophobic C-terminal part of the Aβ-peptide, EM micrographs reveal small crystalline areas (100 to 150 nm, repeating unit 47 Å) scattered in more amorphous material. On a longer time scale, these crystalline areas disappear and are replaced by tangled clusters resembling protofilaments (hours), and eventually by more regular amyloid fibrils of 60 Å to 120 Å diameter (days). The transient population of the crystalline areas indicates the presence of ordered substructures in the early fibrillation process, the diameter of which matches the length of the 14-mer peptide in an extended β-strand conformation.

AB - During the first few minutes of fibrillation of a 14-residue peptide homologous to the hydrophobic C-terminal part of the Aβ-peptide, EM micrographs reveal small crystalline areas (100 to 150 nm, repeating unit 47 Å) scattered in more amorphous material. On a longer time scale, these crystalline areas disappear and are replaced by tangled clusters resembling protofilaments (hours), and eventually by more regular amyloid fibrils of 60 Å to 120 Å diameter (days). The transient population of the crystalline areas indicates the presence of ordered substructures in the early fibrillation process, the diameter of which matches the length of the 14-mer peptide in an extended β-strand conformation.

KW - Amyloid fibrils

KW - Electron microscopy

KW - Peptide aggregation

KW - Peptide crystal

KW - Protein aggregation

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M3 - Journal article

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SP - 1417

EP - 1421

JO - Protein Science

JF - Protein Science

IS - 5

ER -

Transient formation of nano-crystalline structures during fibrillation of an Aβ-like peptide

Abstract

Keywords

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