'Nature-inspired' drug-protein complexes as inhibitors of Abeta aggregation.

Abstract:

:Protein-protein interactions are a regulatory mechanism for a number of physiological and pathological cellular processes. Neurodegenerative diseases, such as AD (Alzheimer's disease), are associated with the accelerated production or delayed clearance of protein aggregates. Hence, inhibition of pathologic protein-protein interactions is a very attractive mechanism for drug development. This review focuses on a novel therapeutic strategy to inhibit the de novo formation of protein aggregates. Inspired by strategies used in Nature and optimized over millions of years of evolution, we have created a bifunctional molecule [SLF (synthetic ligand for FK506-binding protein)-CR (Congo Red)] that is able to block Abeta (amyloid beta) aggregation by borrowing the surface and steric bulk of a cellular chaperone.

journal_name

Biochem Soc Trans

authors

Bose M,Gestwicki JE,Devasthali V,Crabtree GR,Graef IA

doi

10.1042/BST0330543

keywords:

subject

Has Abstract

pub_date

2005-08-01 00:00:00

pages

543-7

issue

Pt 4

eissn

0300-5127

issn

1470-8752

pii

BST0330543

journal_volume

33

pub_type

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