New insights into the mechanisms of protein misfolding and aggregation in amyloidogenic diseases derived from pressure studies
New insights into the mechanisms of protein misfolding and aggregation in amyloidogenic diseases derived from pressure studies
Engineering Village 2
2006 Elsevier Inc.
Accession number: 04388367394
Title: New insights into the mechanisms of protein misfolding and aggregation in amyloidogenic diseases derived from pressure studies
Authors: Foguel, Debora; Silva, Jerson L.
Author affiliation: Univ. Federal do Rio de Janeiro, Depto. de Bioquimica Medica-ICB-CCS, Cidade Universitaria, 21941-590 Rio de Janeiro, RJ, Brazil
Serial title: Biochemistry
Abbreviated serial title: Biochemistry
Volume: v 43
Issue: n 36
Issue date: Sep 14 2004
Publication year: 2004
Pages: p 11361-11370
Language: English
ISSN: 0006-2960
CODEN: BICHAW
Document type: Journal article (JA)
Publisher: American Chemical Society, Columbus, United States
Abstract: Hydrostatic pressure is a robust tool for studying the thermodynamics of protein folding and protein interactions, as well as the dynamics and structure of folding intermediates. One of the main innovations obtained from using high pressure is the stabilization of folding intermediates such as molten-globule conformations, thus providing a unique opportunity for characterizing their structure and dynamics. Equally important is the prospect of understanding protein misfolding diseases by using pressure to populate partially folded intermediates at the junction between productive and off-pathway folding, which may give rise to misfolded proteins, aggregates, and amyloids. High hydrostatic pressure (HHP) has also been used to dissociate nonamyloid aggregates and inclusion bodies. In many proteins, the competition between correct folding and misfolding can lead to formation of insoluble aggregates, an important problem for the biotechnology industry and for human pathologies such as amyloidosis, Alzheimer's, Parkinson's, prion's, and tumor diseases. The diversity of diseases that result from protein misfolding has made this theme an important research focus for pharmaceutical and biotechnology companies. The use of high-pressure promises to contribute to the identification of the mechanisms behind these defects and creation of therapies against these diseases.
Number of references: 76
Ei main heading: Proteins
Ei controlled terms: Agglomeration - Hydrostatic pressure - Thermodynamics - High pressure effects - Biotechnology - Diseases - Pathology - Drug products
Uncontrolled terms: Amyloids - Protein interaction - Insoluble aggregates
Ei classification codes: 804.1 Organic Compounds - 631.1.1 Liquid Dynamics - 641.1 Thermodynamics - 931.2 Physical Properties of Gases, Liquids & Solids - 461.8 Biotechnology - 461.6 Medicine
Treatment: Theoretical (THR)
DOI: 10.1021/bi048864a
Database: Compendex
Compilation and indexing terms, ? 2006 Elsevier Inc. All rights reserved
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