Authors:
Elena Parfenyuk Institution of Russian Academy of Sciences Institute of Solution Chemistry of the RAS Ivanovo Russia

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Galina Kulikova Institution of Russian Academy of Sciences Institute of Solution Chemistry of the RAS Ivanovo Russia

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Irina Ryabinina Institution of Russian Academy of Sciences Institute of Solution Chemistry of the RAS Ivanovo Russia

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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 (Td) 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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Journal of Thermal Analysis and Calorimetry
Language English
Size A4
Year of
Foundation
1969
Volumes
per Year
1
Issues
per Year
24
Founder Akadémiai Kiadó
Founder's
Address
H-1117 Budapest, Hungary 1516 Budapest, PO Box 245.
Publisher Akadémiai Kiadó
Springer Nature Switzerland AG
Publisher's
Address
H-1117 Budapest, Hungary 1516 Budapest, PO Box 245.
CH-6330 Cham, Switzerland Gewerbestrasse 11.
Responsible
Publisher
Chief Executive Officer, Akadémiai Kiadó
ISSN 1388-6150 (Print)
ISSN 1588-2926 (Online)

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