Adsorption/desorption behavior and covalent grafting of an antibody onto cationic amino-functionalized poly(styrene-N-isopropylacrylamide) core-shell latex particles

被引：67

作者：

Taniguchi, T ^{[1
]}

Duracher, D ^{[1
]}

Delair, T ^{[1
]}

Elaïssari, A ^{[1
]}

Pichot, C ^{[1
]}

机构：

[1] Ecole Normale Super Lyon, Unite Mixte CNRS BioMerieux UMR 2142, F-69364 Lyon 07, France

来源：

COLLOIDS AND SURFACES B-BIOINTERFACES | 2003年 / 29卷 / 01期

关键词：

adsorption; desorption; covalent grafting; anti-alpha-feto protein antibody; core-shell latex particle; polystyrene; poly(N-isopropylacrylamide);

D O I：

10.1016/S0927-7765(02)00176-5

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

摘要：

The adsorption of anti-a-feto protein (anti-AFP) onto polystyrene-core-poly(N-isopropylacrylamide)-shell particles was investigated as a function of temperature, pH, and salinity. The influence of various physicochemical parameters onto the colloidal and surface properties of such stimuli-responsive particles was first studied. Then, the adsorption of anti-AFP antibody was investigated in order to point out the driving forces involved in the adsorption process. The effects of salinity, pH, and temperature demonstrated that adsorption was mainly governed by electrostatic interactions. In addition, the adsorption isotherms were analyzed on the basis of a Langmuir model leading to the determination of affinity constants. Finally, based on this adsorption study, various covalent coupling methodologies of the antibody were compared by using two different copolymers as a reactive spacer arm. The amount of chemically grafted antibody was obtained after performing the desorption step (by lowering the temperature, changing the pH, or raising ionic strength). The grafted quantity of antibody was found to be related to the adsorbed amount as a function of pH and ionic strength. (C) 2002 Elsevier Science B.V. All rights reserved.

引用

页码：53 / 65

页数：13

共 30 条

[1] ADSORPTION-KINETICS OF PROTEINS ONTO SOLID-SURFACES IN THE LIMIT OF THE INTERFACIAL INTERACTION CONTROL [J].

APTEL, JD ;

VOEGEL, JC ;

SCHMITT, A .

COLLOIDS AND SURFACES, 1988, 29 (04) :359-371

[2] POLYMER PROTEIN CONJUGATES .1. EFFECT OF PROTEIN CONJUGATION ON THE CLOUD POINT OF POLY(N-ISOPROPYLACRYLAMIDE) [J].

CHEN, JP ;

YANG, HJ ;

HOFFMAN, AS .

BIOMATERIALS, 1990, 11 (09) :625-630

[3]

DAGOSTO F, 2001, THESIS U C BERNARD L

[4] ADSORPTION OF HUMAN-ALBUMIN AND FIBRINOGEN ONTO HEPARIN-LIKE MATERIALS .1. ADSORPTION-ISOTHERMS [J].

DEBAILLOU, N ;

VOEGEL, JC ;

SCHMITT, A .

COLLOIDS AND SURFACES, 1985, 16 (3-4) :271-288

[5] SYNTHESIS AND CHARACTERIZATION OF CATIONIC AMINO FUNCTIONALIZED POLYSTYRENE LATEXES [J].

DELAIR, T ;

MARGUET, V ;

PICHOT, C ;

MANDRAND, B .

COLLOID AND POLYMER SCIENCE, 1994, 272 (08) :962-970

[6] Adsorption of modified HIV-1 capsid p24 protein onto thermosensitive and cationic core-shell poly(styrene)-poly(N-isopropylacrylamide) particles [J].

Duracher, D ;

Elaïssari, A ;

Mallet, F ;

Pichot, C .

LANGMUIR, 2000, 16 (23) :9002-9008

[7]

Duracher D, 1999, J POLYM SCI POL CHEM, V37, P1823

[8] Cationic amino-containing N-isopropylacrylamide-styrene copolymer latex particles: 1 - Particle size and morphology vs. polymerization process [J].

Duracher, D ;

Sauzedde, F ;

Elaissari, A ;

Perrin, A ;

Pichot, C .

COLLOID AND POLYMER SCIENCE, 1998, 276 (03) :219-231

[9] Cationic amino-containing N-isopropyl-acrylamide-styrene copolymer particles: 2-surface and colloidal characteristics [J].

Duracher, D ;

Sauzedde, F ;

Elaissari, A ;

Pichot, C ;

Nabzar, L .

COLLOID AND POLYMER SCIENCE, 1998, 276 (10) :920-929

[10] THE ADSORPTION OF BOVINE SERUM-ALBUMIN ON POSITIVELY AND NEGATIVELY CHARGED POLYSTYRENE LATTICES [J].

ELGERSMA, AV ;

ZSOM, RLJ ;

NORDE, W ;

LYKLEMA, J .

JOURNAL OF COLLOID AND INTERFACE SCIENCE, 1990, 138 (01) :145-156

← 1 2 3 →