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Structural Stability of Myoglobin in Organic Media

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Abstract

The structural stability of metmyoglobin in organic solvents and cosolvents was investigated aiming the choice of a suitable medium to perform its dissolution with maintenance of the native folding. The spectroscopic behavior of metmyoglobin solution in UV–Visible and circular dichroism was used to evaluate the solubility and the secondary structure. The results were dependable of the chemical structure of the organic compounds, their polarity and content, in the case of cosolvents. Protic solvents showed better ability than the aprotic ones for the biomolecule dissolution, since they are able to establish hydrogen bonds. Solvents with high polarity usually damage the secondary structure of the protein. Myoglobin was dissolved in pure methanol, ethylene glycol and glycerol. The secondary structure was retained in some extent. The controlled addition of sodium dodecyl sulfate to myoglobin aqueous solution changed the surface moiety of the protein. The complex was extracted to hexane with efficiency of 77%.

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Abbreviations

CD:

Circular dichroism

SDS:

Sodium dodecyl sulfate

C50 :

Threshold content of the organic cosolvent in which myoglobin is able to retain its native folding

PBS:

Phosphate buffer solution

DMSO:

Dimethyl sulfoxide

Metmb:

Metmyoglobin

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Acknowledgments

The authors would like to thank Capes and CNPQ for the financial support.

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Authors and Affiliations

  1. Chemical Engineering Program-COPPE, Federal University of Rio de Janeiro, P.O. Box 68502, Rio de Janeiro, RJ, 21941-972, Brazil

    Katia C. S. Figueiredo, Helen C. Ferraz, Cristiano P. Borges & Tito L. M. Alves

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  1. Katia C. S. Figueiredo
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  2. Helen C. Ferraz
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  3. Cristiano P. Borges
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  4. Tito L. M. Alves
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Correspondence to Katia C. S. Figueiredo.

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Figueiredo, K.C.S., Ferraz, H.C., Borges, C.P. et al. Structural Stability of Myoglobin in Organic Media. Protein J 28, 224–232 (2009). https://doi.org/10.1007/s10930-009-9187-y

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