Toshiyuki Okuno ^1 2, Yutaka Yoshida ¹, Yuriko Takaki ¹, Yasuyuki Araki ¹, Hironobu Inoue ³, Kazuaki Soejima ^1 3, Yuki Okado ⁴, Kenichi Yoshida ⁴, Haruo Imamura ⁴, Satoshi Hagiwara ⁵, Shigekiyo Matsumoto ⁶, Takaaki Kitano ⁶ , Ther Apher Dial. 2019 Jun;23(3):210-216.

Our findings suggest that granulocytes contact and adhere to each other at the surface layer after adsorption, and that granulocyte-granulocyte adhesion is enhanced by a higher inflammatory response.

https://pubmed.ncbi.nlm.nih.gov/31025504/

Ziwei Huang ¹, Vikram Singh Raghuwanshi ¹, Gil Garnier ¹Front Bioeng Biotechnol. 2017 Jul 17:5:41. doi: 10.3389/fbioe.2017.00041

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.

Functionality of Immunoglobulin G and Immunoglobulin M Antibody Physisorbed on Cellulosic Films – PubMed (nih.gov)

Functionality of Immunoglobulin G and Immunoglobulin M Antibody Physisorbed on Cellulosic Films – PMC (nih.gov)

Muhammad Ali Muzammil ¹, Fnu Fariha ², Tirath Patel ³, Rohab Sohail ⁴, Munesh Kumar ⁵, Ejaz Khan ⁶, Bushra Khanam ⁷, Satesh Kumar ⁸, Mahima Khatri ⁹, Giustino Varrassi ¹⁰, Prasanthi Vanga ¹¹2023 Jun 28;15(6):e41120. doi: 10.7759/cureus.41120.

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.

Functionality of Immunoglobulin G and Immunoglobulin M Antibody Physisorbed on Cellulosic Films – PubMed (nih.gov)