A thermodynamic study of the binding of human serum albumin onto N,N′-diethylaminoethyl dextran microbeads

Hatice Kaplan Can; Ali Güner

doi:10.1002/app.22894

A thermodynamic study of the binding of human serum albumin onto N,N′-diethylaminoethyl dextran microbeads

Hatice Kaplan Can
, Ali Güner

Division of Polymer Chemistry

Hacettepe University

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

2 Citations (Scopus)

Abstract

Adsorption of proteins on solid surfaces is widely studied because of its importance in various biotechnological, medical, and technical applications, e.g., biosensors, cardiovascular implants, and chromatography. Adsorption thermodynamics has been studied on the microbeads of N,N′- diethylaminoethyl (DEAE) Dextran anion exchanger for the human serum albumin (HSA) at 25, 30, 35, 40, and 45°C. As a result, some thermodynamic parameters like Freundlich constants, thermodynamic equilibrium constant (K _D), standard free energy changes (ΔG_assoc), standard entropy changes (ΔS_assoc), and standard enthalpy change (ΔH_assoc) have been evaluated. Using the linear Van't Hoff plot, ΔH_assoc value of the system for the interaction of bovine serum albumin (BSA)-adsorbed crosslinked DEAE dextran microbeads was determined as 20,650 kJ/mol.

Original language	English
Pages (from-to)	3942-3947
Number of pages	6
Journal	Journal of Applied Polymer Science
Volume	101
Issue number	6
DOIs	https://doi.org/10.1002/app.22894
Publication status	Published - 15 Sept 2006

Keywords

Adsorption
Binding energy
Human serum albumin (HSA)
Ion-exchangers
Polysaccharides
UV-vis spectroscopy

Access to Document

10.1002/app.22894

Cite this

@article{a4f3dc8a7c5c416ea83c793067aff144,

title = "A thermodynamic study of the binding of human serum albumin onto N,N′-diethylaminoethyl dextran microbeads",

abstract = "Adsorption of proteins on solid surfaces is widely studied because of its importance in various biotechnological, medical, and technical applications, e.g., biosensors, cardiovascular implants, and chromatography. Adsorption thermodynamics has been studied on the microbeads of N,N′- diethylaminoethyl (DEAE) Dextran anion exchanger for the human serum albumin (HSA) at 25, 30, 35, 40, and 45°C. As a result, some thermodynamic parameters like Freundlich constants, thermodynamic equilibrium constant (K D), standard free energy changes (ΔGassoc), standard entropy changes (ΔSassoc), and standard enthalpy change (ΔHassoc) have been evaluated. Using the linear Van't Hoff plot, ΔHassoc value of the system for the interaction of bovine serum albumin (BSA)-adsorbed crosslinked DEAE dextran microbeads was determined as 20,650 kJ/mol.",

keywords = "Adsorption, Binding energy, Human serum albumin (HSA), Ion-exchangers, Polysaccharides, UV-vis spectroscopy",

author = "Can, \{Hatice Kaplan\} and Ali G{\"u}ner",

year = "2006",

month = sep,

day = "15",

doi = "10.1002/app.22894",

language = "English",

volume = "101",

pages = "3942--3947",

journal = "Journal of Applied Polymer Science",

issn = "0021-8995",

publisher = "John Wiley \& Sons Inc.",

number = "6",

}

TY - JOUR

T1 - A thermodynamic study of the binding of human serum albumin onto N,N′-diethylaminoethyl dextran microbeads

AU - Can, Hatice Kaplan

AU - Güner, Ali

PY - 2006/9/15

Y1 - 2006/9/15

N2 - Adsorption of proteins on solid surfaces is widely studied because of its importance in various biotechnological, medical, and technical applications, e.g., biosensors, cardiovascular implants, and chromatography. Adsorption thermodynamics has been studied on the microbeads of N,N′- diethylaminoethyl (DEAE) Dextran anion exchanger for the human serum albumin (HSA) at 25, 30, 35, 40, and 45°C. As a result, some thermodynamic parameters like Freundlich constants, thermodynamic equilibrium constant (K D), standard free energy changes (ΔGassoc), standard entropy changes (ΔSassoc), and standard enthalpy change (ΔHassoc) have been evaluated. Using the linear Van't Hoff plot, ΔHassoc value of the system for the interaction of bovine serum albumin (BSA)-adsorbed crosslinked DEAE dextran microbeads was determined as 20,650 kJ/mol.

AB - Adsorption of proteins on solid surfaces is widely studied because of its importance in various biotechnological, medical, and technical applications, e.g., biosensors, cardiovascular implants, and chromatography. Adsorption thermodynamics has been studied on the microbeads of N,N′- diethylaminoethyl (DEAE) Dextran anion exchanger for the human serum albumin (HSA) at 25, 30, 35, 40, and 45°C. As a result, some thermodynamic parameters like Freundlich constants, thermodynamic equilibrium constant (K D), standard free energy changes (ΔGassoc), standard entropy changes (ΔSassoc), and standard enthalpy change (ΔHassoc) have been evaluated. Using the linear Van't Hoff plot, ΔHassoc value of the system for the interaction of bovine serum albumin (BSA)-adsorbed crosslinked DEAE dextran microbeads was determined as 20,650 kJ/mol.

KW - Adsorption

KW - Binding energy

KW - Human serum albumin (HSA)

KW - Ion-exchangers

KW - Polysaccharides

KW - UV-vis spectroscopy

UR - https://www.scopus.com/pages/publications/33748307489

U2 - 10.1002/app.22894

DO - 10.1002/app.22894

M3 - Article

AN - SCOPUS:33748307489

SN - 0021-8995

VL - 101

SP - 3942

EP - 3947

JO - Journal of Applied Polymer Science

JF - Journal of Applied Polymer Science

IS - 6

ER -

A thermodynamic study of the binding of human serum albumin onto N,N′-diethylaminoethyl dextran microbeads

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Cite this