Amyloid beta (1-42) folding multiplicity and single-molecule binding behavior studied with STM.

Abstract:

:The fine folding and assembling characteristics of amyloid beta (Abeta) peptides are important to pharmaceutical studies of drug molecules and to the pathological analysis of neurodegenerative disorders such as Alzheimer's disease at the molecular level. Here we present observations of the multiple folding characteristics of amyloid peptide Abeta(42) lamellae using scanning tunneling microscopy. Molecularly resolved core regions of Abeta(42) hairpins and unfolded peptide assembly structures are identified. The parallel assembling characteristics of Abeta(42) hairpins can be confirmed in the study. In addition, single-molecule binding characteristics of Congo red and thioflavin T have been shown to bind at the groove regions of peptide assemblies. This study demonstrates a complementary venue for studying molecular heterogeneity of peptide assemblies, as well as the binding characteristics of molecular modulators.

journal_name

J Mol Biol

authors

Ma X,Liu L,Mao X,Niu L,Deng K,Wu W,Li Y,Yang Y,Wang C

doi

10.1016/j.jmb.2009.03.054

subject

Has Abstract

pub_date

2009-05-15 00:00:00

pages

894-901

issue

4

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(09)00340-4

journal_volume

388

pub_type

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