Non-pretreated O-acyl isopeptide of amyloid β peptide 1-42 is monomeric with a random coil structure but starts to aggregate in a concentration-dependent manner.

Authors :: Yoshiya T
Maruno T
Uemura T
Kubo S
Kiso Y
Sohma Y
Yoshizawa-Kumagaye K
Kobayashi Y
Nishiuchi Y
Source :: Bioorganic & medicinal chemistry letters [Bioorg Med Chem Lett] 2014 Aug 15; Vol. 24 (16), pp. 3861-4. Date of Electronic Publication: 2014 Jun 25.
Publication Year :: 2014
Abstract: An isopeptide of amyloid β peptide 1-42 (isoAβ42) was considered as a non-aggregative precursor molecule for the highly aggregative Aβ42. It has been applied to biological studies after several pretreatments. Here we report that isoAβ42 is monomeric with a random coil structure at 40 μM without any pretreatment. But we also found that isoAβ42 retains a slight aggregative nature, which is significantly weaker than that of the native Aβ42.<br /> (Copyright © 2014 The Authors. Published by Elsevier Ltd.. All rights reserved.)

Subjects :: Protein Conformation
Amyloid beta-Peptides chemistry
Peptide Fragments chemistry

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