Document Detail

Pressure dependence of human fibrinogen correlated to the conformational alpha-helix to beta-sheet transition: an Fourier transform infrared study microspectroscopic study.
MedLine Citation:
PMID:  15457437     Owner:  NLM     Status:  MEDLINE    
We used Fourier transform infrared (FTIR) microspectroscopy to investigate pressure-induced conformational changes in secondary structure of fibrinogen (FBG). Solid state FBG was compressed on a KBr pellet (1KBr method) or between two KBr pellets (2KBr method). The peak positions of the original and second-derivative ir spectra of compressed FBG samples prepared by the 1KBr method were similar to FBG sample without pressure. When FBG was prepared by the 2KBr method and pressure was increased up to 400 kg/cm(2), peaks at 1625 (intermolecular beta-sheet) and 1611 (beta-sheet aggregates structure and/or the side-chain absorption of the tyrosine residues) cm(-1) were enhanced. The peaks near 1661 (beta-sheet) and 1652 (alpha-helix) cm(-1) also exhibited a marked change with pressure. A linear correlation was found between the peak intensity ratio of 1611/1652 cm(-1) (r = 0.9879) or 1625/1652 cm(-1) (r = 0.9752) and applied pressure. The curve-fitted compositional changes in secondary structure of FBG also indicate that the composition of the alpha-helix structure (1657-1659 cm(-1)) was gradually reduced with the increase in compression pressure, but the composition of the beta-sheet structure (1681, 1629, and 1609 cm(-1)) gradually increased. This indicates that pressure-induced conformational changes in FBG include not only transformations from alpha-helix to beta-sheet structure, but also unfolding and denaturation of FBG and the formation of aggregates.
Shan-Yang Lin; Yen-Shan Wei; Tzu-Feng Hsieh; Mei-Jane Li
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Biopolymers     Volume:  75     ISSN:  0006-3525     ISO Abbreviation:  Biopolymers     Publication Date:  2004 Dec 
Date Detail:
Created Date:  2004-11-03     Completed Date:  2005-03-07     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0372525     Medline TA:  Biopolymers     Country:  United States    
Other Details:
Languages:  eng     Pagination:  393-402     Citation Subset:  IM    
Copyright Information:
Copyright 2004 Wiley Periodicals, Inc.
Biopharmaceutics Laboratory, Department of Medical Research and Education, Veterans General Hospital-Taipei, Taipei, Taiwan, Republic of China.
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MeSH Terms
Fibrinogen / chemistry*
Protein Structure, Secondary
Spectroscopy, Fourier Transform Infrared
Reg. No./Substance:

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