Home > Research > Publications & Outputs > The immunoreactive profile at the N-terminal re...

Research

Links

Text available via DOI:

Keywords

View graph of relations

The immunoreactive profile at the N-terminal region of Aβ1-39/40 but not Aβ1-42 changes with transition from monomer/dimer to further peptide aggregates

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Published

Standard

The immunoreactive profile at the N-terminal region of Aβ1-39/40 but not Aβ1-42 changes with transition from monomer/dimer to further peptide aggregates. / Kametani, F; Tanaka, K; Tokuda, T et al.
In: Brain Research, Vol. 703, No. 1-2, 12.12.1995, p. 237-241.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Harvard

Kametani, F, Tanaka, K, Tokuda, T & Allsop, D 1995, 'The immunoreactive profile at the N-terminal region of Aβ1-39/40 but not Aβ1-42 changes with transition from monomer/dimer to further peptide aggregates', Brain Research, vol. 703, no. 1-2, pp. 237-241. https://doi.org/10.1016/0006-8993(95)01195-1

APA

Kametani, F., Tanaka, K., Tokuda, T., & Allsop, D. (1995). The immunoreactive profile at the N-terminal region of Aβ1-39/40 but not Aβ1-42 changes with transition from monomer/dimer to further peptide aggregates. Brain Research, 703(1-2), 237-241. https://doi.org/10.1016/0006-8993(95)01195-1

Vancouver

Kametani F, Tanaka K, Tokuda T, Allsop D. The immunoreactive profile at the N-terminal region of Aβ1-39/40 but not Aβ1-42 changes with transition from monomer/dimer to further peptide aggregates. Brain Research. 1995 Dec 12;703(1-2):237-241. doi: 10.1016/0006-8993(95)01195-1

Author

Kametani, F ; Tanaka, K ; Tokuda, T et al. / The immunoreactive profile at the N-terminal region of Aβ1-39/40 but not Aβ1-42 changes with transition from monomer/dimer to further peptide aggregates. In: Brain Research. 1995 ; Vol. 703, No. 1-2. pp. 237-241.

Bibtex

@article{390007c8f8ba4051b39ebb194c7f1f26,
title = "The immunoreactive profile at the N-terminal region of Aβ1-39/40 but not Aβ1-42 changes with transition from monomer/dimer to further peptide aggregates",
abstract = "Using site-specific antibodies, we assessed the effect of aggregation of various length forms of A beta on the immunoreactive profile of the peptides. All of the antibodies tested reacted with monomeric/dimeric forms of A beta 1-42 and its further aggregates. However, antibodies directed against the 1-24 region of A beta reacted weakly or not at all with A beta 1-39/40 monomers or dimers, but immunoreactivity was enhanced substantially following peptide incubation and aggregation. These results suggest that the conformation of the N-terminal region of monomeric and dimeric A beta 1-39/40 is different from that of aggregated forms, whereas the longer A beta 1-42 does not significantly change its N-terminal conformation during beta-sheet fibril formation. These immunochemical results are consistent with previous structural data, and help to explain the differential effects of A beta 1-39/40 and 1-42 on fibril formation in brain.",
keywords = "Blotting, Western, Immunoenzyme Techniques, Peptide Fragments, Protein Conformation",
author = "F Kametani and K Tanaka and T Tokuda and D Allsop",
year = "1995",
month = dec,
day = "12",
doi = "10.1016/0006-8993(95)01195-1",
language = "English",
volume = "703",
pages = "237--241",
journal = "Brain Research",
issn = "0006-8993",
publisher = "Elsevier",
number = "1-2",

}

RIS

TY - JOUR

T1 - The immunoreactive profile at the N-terminal region of Aβ1-39/40 but not Aβ1-42 changes with transition from monomer/dimer to further peptide aggregates

AU - Kametani, F

AU - Tanaka, K

AU - Tokuda, T

AU - Allsop, D

PY - 1995/12/12

Y1 - 1995/12/12

N2 - Using site-specific antibodies, we assessed the effect of aggregation of various length forms of A beta on the immunoreactive profile of the peptides. All of the antibodies tested reacted with monomeric/dimeric forms of A beta 1-42 and its further aggregates. However, antibodies directed against the 1-24 region of A beta reacted weakly or not at all with A beta 1-39/40 monomers or dimers, but immunoreactivity was enhanced substantially following peptide incubation and aggregation. These results suggest that the conformation of the N-terminal region of monomeric and dimeric A beta 1-39/40 is different from that of aggregated forms, whereas the longer A beta 1-42 does not significantly change its N-terminal conformation during beta-sheet fibril formation. These immunochemical results are consistent with previous structural data, and help to explain the differential effects of A beta 1-39/40 and 1-42 on fibril formation in brain.

AB - Using site-specific antibodies, we assessed the effect of aggregation of various length forms of A beta on the immunoreactive profile of the peptides. All of the antibodies tested reacted with monomeric/dimeric forms of A beta 1-42 and its further aggregates. However, antibodies directed against the 1-24 region of A beta reacted weakly or not at all with A beta 1-39/40 monomers or dimers, but immunoreactivity was enhanced substantially following peptide incubation and aggregation. These results suggest that the conformation of the N-terminal region of monomeric and dimeric A beta 1-39/40 is different from that of aggregated forms, whereas the longer A beta 1-42 does not significantly change its N-terminal conformation during beta-sheet fibril formation. These immunochemical results are consistent with previous structural data, and help to explain the differential effects of A beta 1-39/40 and 1-42 on fibril formation in brain.

KW - Blotting, Western

KW - Immunoenzyme Techniques

KW - Peptide Fragments

KW - Protein Conformation

U2 - 10.1016/0006-8993(95)01195-1

DO - 10.1016/0006-8993(95)01195-1

M3 - Journal article

C2 - 8719640

VL - 703

SP - 237

EP - 241

JO - Brain Research

JF - Brain Research

SN - 0006-8993

IS - 1-2

ER -