Native and hydrophobized human IgG enthalpies of heat-induced structural changes and adsorption onto silica

A. Kamyshny; P. Relkin; S. Lagerge; S. Partyka; S. Magdassi

Native and hydrophobized human IgG enthalpies of heat-induced structural changes and adsorption onto silica

A. Kamyshny^*, P. Relkin, S. Lagerge, S. Partyka, S. Magdassi

^*Corresponding author for this work

Institute of Chemistry

Research output: Contribution to journal › Article › peer-review

3 Scopus citations

Abstract

Differential scanning calorimetry (DSC) and isothermal calorimetric batch technique were used to monitor the heat-induced structural changes and adsorption properties of human immunoglobulin G (IgG), in native and hydrophobized states. The transition temperature (T_max) and enthalpy of heat-induced conformational changes (Δ_calH) of IgG in solution as well as the enthalpy change accompanying the adsorption of IgG onto hydrophilic silica (Δ_adsH), were shown to depend on the degree of the protein hydrophobicity (number of covalently attached alkyl chains). The adsorption enthalpy for all forms of IgG at all surface concentrations was found to be endothermic, that is the process is entropy driven. Factors affecting the IgG adsorption onto silica are discussed.

Original language	English
Pages (from-to)	263-272
Number of pages	10
Journal	Journal of Thermal Analysis and Calorimetry
Volume	71
Issue number	1
State	Published - 2003

Bibliographical note

Funding Information:
This collaborative study was partially supported by ARIEL and carried out in the frame of Arc-en-Ciel (Keshet) program between Israel and France.

Keywords

Enthalpy of adsorption
Human IgG
Structural changes

Cite this

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abstract = "Differential scanning calorimetry (DSC) and isothermal calorimetric batch technique were used to monitor the heat-induced structural changes and adsorption properties of human immunoglobulin G (IgG), in native and hydrophobized states. The transition temperature (Tmax) and enthalpy of heat-induced conformational changes (ΔcalH) of IgG in solution as well as the enthalpy change accompanying the adsorption of IgG onto hydrophilic silica (ΔadsH), were shown to depend on the degree of the protein hydrophobicity (number of covalently attached alkyl chains). The adsorption enthalpy for all forms of IgG at all surface concentrations was found to be endothermic, that is the process is entropy driven. Factors affecting the IgG adsorption onto silica are discussed.",

keywords = "Enthalpy of adsorption, Human IgG, Structural changes",

author = "A. Kamyshny and P. Relkin and S. Lagerge and S. Partyka and S. Magdassi",

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T1 - Native and hydrophobized human IgG enthalpies of heat-induced structural changes and adsorption onto silica

AU - Kamyshny, A.

AU - Relkin, P.

AU - Lagerge, S.

AU - Partyka, S.

AU - Magdassi, S.

N1 - Funding Information: This collaborative study was partially supported by ARIEL and carried out in the frame of Arc-en-Ciel (Keshet) program between Israel and France.

PY - 2003

Y1 - 2003

N2 - Differential scanning calorimetry (DSC) and isothermal calorimetric batch technique were used to monitor the heat-induced structural changes and adsorption properties of human immunoglobulin G (IgG), in native and hydrophobized states. The transition temperature (Tmax) and enthalpy of heat-induced conformational changes (ΔcalH) of IgG in solution as well as the enthalpy change accompanying the adsorption of IgG onto hydrophilic silica (ΔadsH), were shown to depend on the degree of the protein hydrophobicity (number of covalently attached alkyl chains). The adsorption enthalpy for all forms of IgG at all surface concentrations was found to be endothermic, that is the process is entropy driven. Factors affecting the IgG adsorption onto silica are discussed.

AB - Differential scanning calorimetry (DSC) and isothermal calorimetric batch technique were used to monitor the heat-induced structural changes and adsorption properties of human immunoglobulin G (IgG), in native and hydrophobized states. The transition temperature (Tmax) and enthalpy of heat-induced conformational changes (ΔcalH) of IgG in solution as well as the enthalpy change accompanying the adsorption of IgG onto hydrophilic silica (ΔadsH), were shown to depend on the degree of the protein hydrophobicity (number of covalently attached alkyl chains). The adsorption enthalpy for all forms of IgG at all surface concentrations was found to be endothermic, that is the process is entropy driven. Factors affecting the IgG adsorption onto silica are discussed.

KW - Enthalpy of adsorption

KW - Human IgG

KW - Structural changes

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SN - 1388-6150

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JO - Journal of Thermal Analysis and Calorimetry

JF - Journal of Thermal Analysis and Calorimetry

IS - 1

ER -

Native and hydrophobized human IgG enthalpies of heat-induced structural changes and adsorption onto silica

Abstract

Bibliographical note

Keywords

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