Literature DB >> 23277670

New insights into bioprotective effectiveness of disaccharides: an FTIR study of human haemoglobin aqueous solutions exposed to static magnetic fields.

Salvatore Magazù1, Emanuele Calabrò, Salvatore Campo, Salvatore Interdonato.   

Abstract

The aim of this study was the investigation of static magnetic field effects on haemoglobin secondary structure and the bioprotective effectiveness of two disaccharides, sucrose and trehalose. Samples of haemoglobin aqueous solutions, in the absence and in the presence of sucrose and trehalose, were exposed to a uniform magnetic field at 200 mT, which is the exposure limit established by the ICNIRP recommendation for occupational exposure. Spectral analysis by FTIR spectroscopy after 3 and 7 h of exposure revealed a decrease in the amide A vibration band for haemoglobin in bi-distilled water solution. Analogue exposures did not produce any appreciable change of amide A for haemoglobin in sucrose and trehalose solutions. Otherwise, no relative increase of [Formula: see text]-sheet contents in amide I and II regions was detected for haemoglobin aqueous solutions, leading us to exclude the hypothesis that static magnetic fields can induce the formation of aggregates in the protein. In addition, a decrease in CH(3) stretching linkages occurred for haemoglobin in bi-distilled water solution after exposure, which was not observed for haemoglobin in sucrose and trehalose aqueous solutions, providing further evidence of a bioprotective compensatory mechanism of such disaccharides.

Entities:  

Keywords:  Disaccharides; Electromagnetic field; Haemoglobin; Infrared spectroscopy; Static magnetic field; Trehalose

Year:  2011        PMID: 23277670      PMCID: PMC3285734          DOI: 10.1007/s10867-010-9209-1

Source DB:  PubMed          Journal:  J Biol Phys        ISSN: 0092-0606            Impact factor:   1.365


  26 in total

1.  Single-pass attenuated total reflection Fourier transform infrared spectroscopy for the analysis of proteins in H2O solution.

Authors:  Brandye M Smith; Stefan Franzen
Journal:  Anal Chem       Date:  2002-08-15       Impact factor: 6.986

2.  FTIR spectroscopy studies on the bioprotective effectiveness of trehalose on human hemoglobin aqueous solutions under 50 Hz electromagnetic field exposure.

Authors:  Salvatore Magazù; Emanuele Calabrò; Salvatore Campo
Journal:  J Phys Chem B       Date:  2010-09-23       Impact factor: 2.991

3.  Thermostabilization mechanism of bovine serum albumin by trehalose.

Authors:  Alain Hédoux; Jean-François Willart; Laurent Paccou; Yannick Guinet; Frédéric Affouard; Adrien Lerbret; Marc Descamps
Journal:  J Phys Chem B       Date:  2009-04-30       Impact factor: 2.991

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Journal:  Ann Occup Hyg       Date:  1998-07

5.  Solid-state stability of human insulin. II. Effect of water on reactive intermediate partitioning in lyophiles from pH 2-5 solutions: stabilization against covalent dimer formation.

Authors:  R G Strickley; B D Anderson
Journal:  J Pharm Sci       Date:  1997-06       Impact factor: 3.534

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Authors:  H Susi; D M Byler
Journal:  Methods Enzymol       Date:  1986       Impact factor: 1.600

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Authors:  D M Byler; H Susi
Journal:  Biopolymers       Date:  1986-03       Impact factor: 2.505

8.  IR and Raman spectroscopic studies of the interaction of trehalose with hen egg white lysozyme.

Authors:  P S Belton; A M Gil
Journal:  Biopolymers       Date:  1994-07       Impact factor: 2.505

9.  Why is trehalose an exceptional protein stabilizer? An analysis of the thermal stability of proteins in the presence of the compatible osmolyte trehalose.

Authors:  Jai K Kaushik; Rajiv Bhat
Journal:  J Biol Chem       Date:  2003-04-17       Impact factor: 5.157

10.  Correlation between bioprotective effectiveness and dynamic properties of trehalose-water, maltose-water and sucrose-water mixtures.

Authors:  S Magazù; F Migliardo; C Mondelli; M Vadalà
Journal:  Carbohydr Res       Date:  2005-10-24       Impact factor: 2.104

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