Literature DB >> 19381627

Protective effect of 3,5,3'-triiodothyroacetic and 3,5,3',5'-tetraiodothyroacetic acids on serum albumin fibrillation.

Leonardo M Cortez1, Ricardo N Farías, Rosana N Chehín.   

Abstract

Inhibition or reversion of protein self-aggregation has been suggested as a possible preventive mechanism against amyloid diseases, and many efforts are underway to found out molecules capable to restrain the protein aggregation process. In this paper, the inhibitory effects of thyroid hormone analogues on heat-induced fibrillation process of serum albumin are reported. Among the analogues tested, 3,5,3',5'-tetraiodothyroacetic and 3,5,3'-triiodothyroacetic acid showed the most important inhibitory effects on amyloid formation. Thyroxine exhibits a lesser protective effect, while 3,5,3'-triiodothyronine showed no significant inhibition. The gaining of a negative charge together with a size reduction of the hormone molecule could play an essential role in the inhibition of fibrils formation. According to infrared spectroscopy results, the thyroid hormones analogues protective effects proceed via the stabilization of the protein native structure. The current work demonstrates the effectiveness of naturally occurring molecules in the inhibition of albumin fibril formation.

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Year:  2009        PMID: 19381627     DOI: 10.1007/s00249-009-0448-7

Source DB:  PubMed          Journal:  Eur Biophys J        ISSN: 0175-7571            Impact factor:   1.733


  40 in total

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Journal:  Nature       Date:  2003-12-18       Impact factor: 49.962

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Journal:  Anal Biochem       Date:  2006-03-27       Impact factor: 3.365

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Journal:  J Med Chem       Date:  2006-10-05       Impact factor: 7.446

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Journal:  J Biol Chem       Date:  1995-04-21       Impact factor: 5.157

Review 5.  Quantitative studies of the structure of proteins in solution by Fourier-transform infrared spectroscopy.

Authors:  J L Arrondo; A Muga; J Castresana; F M Goñi
Journal:  Prog Biophys Mol Biol       Date:  1993       Impact factor: 3.667

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Journal:  J Biol Chem       Date:  1997-09-12       Impact factor: 5.157

7.  Kinetic stabilization of the alpha-synuclein protofibril by a dopamine-alpha-synuclein adduct.

Authors:  K A Conway; J C Rochet; R M Bieganski; P T Lansbury
Journal:  Science       Date:  2001-11-09       Impact factor: 47.728

Review 8.  Zeroing in on the pathogenic form of alpha-synuclein and its mechanism of neurotoxicity in Parkinson's disease.

Authors:  Michael J Volles; Peter T Lansbury
Journal:  Biochemistry       Date:  2003-07-08       Impact factor: 3.162

9.  Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution.

Authors:  H LeVine
Journal:  Protein Sci       Date:  1993-03       Impact factor: 6.725

10.  The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid.

Authors:  Z Lai; W Colón; J W Kelly
Journal:  Biochemistry       Date:  1996-05-21       Impact factor: 3.162

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