UV Resonance Raman Study of TTR(105-115) Structural Evolution as a Function of Temperature

UVRR spectroscopy was used to probe the temperature dependence of the conformation of the 11-residue peptide TTR(105-115) in solution. TTR(105-115) (YTIAALLSPYS) is part of the sequence of the human amyloid-forming protein transthyretin, corresponding to a naturally-occurring b-strand in the crystal...

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Bibliographic Details
Main Authors: Pieridou, G, Avgousti-Menelaou, C, Tamamis, P, Archontis, G, Hayes, S C
Format: Conference Proceeding
Language:English
Online Access:Get full text
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Summary:UVRR spectroscopy was used to probe the temperature dependence of the conformation of the 11-residue peptide TTR(105-115) in solution. TTR(105-115) (YTIAALLSPYS) is part of the sequence of the human amyloid-forming protein transthyretin, corresponding to a naturally-occurring b-strand in the crystal structure of the protein. Transthyretin is a serum protein, produced by the liver, which transports thyroxin and retinol-binding protein. The misfolded mutant of this protein is involved in Familial Amyloid Polyneuropathy (FAP), a lethal disease. This peptide fragment has been shown to form ordered amyloid fibrils in vitro, constituting it an ideal model for the study of fibril formation in general.
ISSN:0094-243X
DOI:10.1063/1.3482862