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DSC and spectroscopic investigation of human serum albumin adsorbed onto silica nanoparticles functionalized by amino groups

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Abstract

Human serum albumin (HSA) adsorbed onto silica nanoparticles modified by 3-aminopropyltriethoxysilane (APTES) and polyethyleneimine (PEI) was investigated by differential scanning calorimetry, IR spectroscopy, and photon correlation spectroscopy. The structural alterations of the protein molecules induced from adsorption process were estimated on the basis of temperatures of denaturation transition (T d) of the protein in free (native) and adsorbed form. It was found that adsorption of the protein onto the APTES-modified silica nanoparticles results in an increase in the temperature of denaturation transition from 42 to 47.4 °C. HSA adsorbed onto the PEI-modified silica nanoparticles unfolds extensively.

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Acknowledgments

This study was supported by a grant from Russian Foundation of Basic Research 09-03-97513.

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Authors and Affiliations

  1. Institution of Russian Academy of Sciences Institute of Solution Chemistry of the RAS, Ivanovo, Russia

    Elena V. Parfenyuk, Galina A. Kulikova & Irina V. Ryabinina

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  1. Elena V. Parfenyuk
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  2. Galina A. Kulikova
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  3. Irina V. Ryabinina
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Correspondence to Elena V. Parfenyuk.

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Parfenyuk, E.V., Kulikova, G.A. & Ryabinina, I.V. DSC and spectroscopic investigation of human serum albumin adsorbed onto silica nanoparticles functionalized by amino groups. J Therm Anal Calorim 100, 987–991 (2010). https://doi.org/10.1007/s10973-009-0604-4

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  • DOI: https://doi.org/10.1007/s10973-009-0604-4

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