Functionality of Immunoglobulin G and Immunoglobulin M Antibody Physisorbed on Cellulosic Films

The functionality and aging mechanism of antibodies physisorbed onto cellulosic films was investigated. Blood grouping antibodies immunoglobulin G (IgG) and immunoglobulin M (IgM) were adsorbed onto smooth cellulose acetate (CAF) and regenerated cellulose (RCF) films. Cellulose films and adsorbed Ig...

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Main Authors: Ziwei Huang, Vikram Singh Raghuwanshi, Gil Garnier
Format: Article
Language:English
Published: Frontiers Media S.A. 2017-07-01
Series:Frontiers in Bioengineering and Biotechnology
Subjects:
Online Access:http://journal.frontiersin.org/article/10.3389/fbioe.2017.00041/full
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author Ziwei Huang
Vikram Singh Raghuwanshi
Gil Garnier
author_facet Ziwei Huang
Vikram Singh Raghuwanshi
Gil Garnier
author_sort Ziwei Huang
collection DOAJ
description The functionality and aging mechanism of antibodies physisorbed onto cellulosic films was investigated. Blood grouping antibodies immunoglobulin G (IgG) and immunoglobulin M (IgM) were adsorbed onto smooth cellulose acetate (CAF) and regenerated cellulose (RCF) films. Cellulose films and adsorbed IgG layers were characterized at the air and liquid interface by X-ray and neutron reflectivity (NR), respectively. Cellulose film 208 Å thick (in air) swell to 386 Å once equilibrated in water. IgG adsorbs from solution onto cellulose as a partial layer 62 Å thick. IgG and IgM antibodies were adsorbed onto cellulose and cellulose acetate films, air dried, and aged at room temperature for periods up to 20 days. Antibody functionality and surface hydrophobicity were measured everyday with the size of red blood cell (RBC) agglutinates (using RBC specific to IgG/IgM) and the water droplet contact angle, respectively. The functionality of the aged IgG/IgM decreases faster if physisorbed on cellulose than on cellulose acetate and correlates to surface hydrophobicity. IgG physisorbed on RCF or CAF age better and remain functional longer than physisorbed IgM. We found a correlation between antibody stability and hydrogen bond formation ability of the system, evaluated from antibody carbonyl concentration and cellulosic surface hydroxyl concentration. Antibody physisorbs on cellulose by weak dipole forces and hydrogen bonds. Strong hydrogen bonding contributes to the physisorption of antibody on cellulose into a non-functional configuration in which the molecule relaxes by rotation of hydophobic groups toward the air interface.
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spelling doaj.art-daddb4fb1cde45aabc39b53ad8e1f6462022-12-22T00:41:21ZengFrontiers Media S.A.Frontiers in Bioengineering and Biotechnology2296-41852017-07-01510.3389/fbioe.2017.00041279423Functionality of Immunoglobulin G and Immunoglobulin M Antibody Physisorbed on Cellulosic FilmsZiwei Huang0Vikram Singh Raghuwanshi1Gil Garnier2Department of Chemical Engineering, Bioresource Processing Institute of Australia (BioPRIA), Monash University, Clayton, VIC, AustraliaDepartment of Chemical Engineering, Bioresource Processing Institute of Australia (BioPRIA), Monash University, Clayton, VIC, AustraliaDepartment of Chemical Engineering, Bioresource Processing Institute of Australia (BioPRIA), Monash University, Clayton, VIC, AustraliaThe functionality and aging mechanism of antibodies physisorbed onto cellulosic films was investigated. Blood grouping antibodies immunoglobulin G (IgG) and immunoglobulin M (IgM) were adsorbed onto smooth cellulose acetate (CAF) and regenerated cellulose (RCF) films. Cellulose films and adsorbed IgG layers were characterized at the air and liquid interface by X-ray and neutron reflectivity (NR), respectively. Cellulose film 208 Å thick (in air) swell to 386 Å once equilibrated in water. IgG adsorbs from solution onto cellulose as a partial layer 62 Å thick. IgG and IgM antibodies were adsorbed onto cellulose and cellulose acetate films, air dried, and aged at room temperature for periods up to 20 days. Antibody functionality and surface hydrophobicity were measured everyday with the size of red blood cell (RBC) agglutinates (using RBC specific to IgG/IgM) and the water droplet contact angle, respectively. The functionality of the aged IgG/IgM decreases faster if physisorbed on cellulose than on cellulose acetate and correlates to surface hydrophobicity. IgG physisorbed on RCF or CAF age better and remain functional longer than physisorbed IgM. We found a correlation between antibody stability and hydrogen bond formation ability of the system, evaluated from antibody carbonyl concentration and cellulosic surface hydroxyl concentration. Antibody physisorbs on cellulose by weak dipole forces and hydrogen bonds. Strong hydrogen bonding contributes to the physisorption of antibody on cellulose into a non-functional configuration in which the molecule relaxes by rotation of hydophobic groups toward the air interface.http://journal.frontiersin.org/article/10.3389/fbioe.2017.00041/fullantibodyimmunoglobulin Gimmunoglobulin Mcellulosephysisorptionfunctionality
spellingShingle Ziwei Huang
Vikram Singh Raghuwanshi
Gil Garnier
Functionality of Immunoglobulin G and Immunoglobulin M Antibody Physisorbed on Cellulosic Films
Frontiers in Bioengineering and Biotechnology
antibody
immunoglobulin G
immunoglobulin M
cellulose
physisorption
functionality
title Functionality of Immunoglobulin G and Immunoglobulin M Antibody Physisorbed on Cellulosic Films
title_full Functionality of Immunoglobulin G and Immunoglobulin M Antibody Physisorbed on Cellulosic Films
title_fullStr Functionality of Immunoglobulin G and Immunoglobulin M Antibody Physisorbed on Cellulosic Films
title_full_unstemmed Functionality of Immunoglobulin G and Immunoglobulin M Antibody Physisorbed on Cellulosic Films
title_short Functionality of Immunoglobulin G and Immunoglobulin M Antibody Physisorbed on Cellulosic Films
title_sort functionality of immunoglobulin g and immunoglobulin m antibody physisorbed on cellulosic films
topic antibody
immunoglobulin G
immunoglobulin M
cellulose
physisorption
functionality
url http://journal.frontiersin.org/article/10.3389/fbioe.2017.00041/full
work_keys_str_mv AT ziweihuang functionalityofimmunoglobulingandimmunoglobulinmantibodyphysisorbedoncellulosicfilms
AT vikramsinghraghuwanshi functionalityofimmunoglobulingandimmunoglobulinmantibodyphysisorbedoncellulosicfilms
AT gilgarnier functionalityofimmunoglobulingandimmunoglobulinmantibodyphysisorbedoncellulosicfilms