当前位置： SCI文献检索 > JOURNAL OF MOLECULAR BIOLOGY期刊下所有文献 > Transthyretin Interferes with Aβ Amyloid Formation by Redirecting Oligomeric Nuclei into Non-Amyloid Aggregates.

Transthyretin Interferes with Aβ Amyloid Formation by Redirecting Oligomeric Nuclei into Non-Amyloid Aggregates.

Abstract：

:The pathological Aβ aggregates associated with Alzheimer's disease follow a nucleation-dependent path of formation. A nucleus represents an oligomeric assembly of Aβ peptides that acts as a template for subsequent incorporation of monomers to form a fibrillar structure. Nuclei can form de novo or via surface-catalyzed secondary nucleation, and the combined rates of elongation and nucleation control the overall rate of fibril formation. Transthyretin (TTR) obstructs Aβ fibril formation in favor of alternative non-fibrillar assemblies, but the mechanism behind this activity is not fully understood. This study shows that TTR does not significantly disturb fibril elongation; rather, it effectively interferes with the formation of oligomeric nuclei. We demonstrate that this interference can be modulated by altering the relative contribution of elongation and nucleation, and we show how TTR's effects can range from being essentially ineffective to almost complete inhibition of fibril formation without changing the concentration of TTR or monomeric Aβ.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Nilsson L,Pamrén A,Islam T,Brännström K,Golchin SA,Pettersson N,Iakovleva I,Sandblad L,Gharibyan AL,Olofsson A

doi

10.1016/j.jmb.2018.06.005

subject

Has Abstract

pub_date

2018-08-17 00:00:00

pages

2722-2733

issue

17

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(18)30581-3

journal_volume

430

pub_type

杂志文章

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