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Light Scattering Study of the Antibody-Poly(methacrylic acid) and Antibody-Poly(acrylic acid) Conjugates in Aqueous Solutions

Kazakov, Sergey V. ; Muronetz, Vladimir I. ; Dainiak, Maria B. LU ; Izumrudov, Vladimir A. LU ; Galaev, Igor Yu LU and Mattiasson, Bo LU (2001) In Macromolecular Bioscience 1(4). p.157-163
Abstract

The effect of the conformational state of the polymer coil on the properties of protein-polymer conjugates has been studied for the conjugates of antibody (monoclonal antibody from 6C5 clone against inactivated rabbit muscle glyceraldehyde-3-phosphate dehydrogenase; Ab) with poly(methacrylic acid) (PMAA) or poly-(acrylic acid) (PAA). The pH-dependencies of molecular properties and structural parameters of aqueous solutions (radius of gyration, intensity of scattered light, hydrodynamic diameter, and polydisperisty index) of Ab, PMAA, and PAA, have been studied using static and dynamic light scattering techniques. While free Ab aggregates in solution and precipitates at its isoelectric point, the covalent attachment of a charged polymer... (More)

The effect of the conformational state of the polymer coil on the properties of protein-polymer conjugates has been studied for the conjugates of antibody (monoclonal antibody from 6C5 clone against inactivated rabbit muscle glyceraldehyde-3-phosphate dehydrogenase; Ab) with poly(methacrylic acid) (PMAA) or poly-(acrylic acid) (PAA). The pH-dependencies of molecular properties and structural parameters of aqueous solutions (radius of gyration, intensity of scattered light, hydrodynamic diameter, and polydisperisty index) of Ab, PMAA, and PAA, have been studied using static and dynamic light scattering techniques. While free Ab aggregates in solution and precipitates at its isoelectric point, the covalent attachment of a charged polymer to Ab prevents its association and shifts the precipitation point towards more acidic values (from pH 5.95 for Ab to pH ∼ 4.8 for Ab- PMAA). The predominant role of the conformational status of the polymer in the process of conjugate precipitation has been considered. Contrary to the precipitation of Ab-PMAA, the formation of stable colloidal particles was suggested for Ab-PAA at pH < 4.8. In the conjugates, polymer chains surround the protein globule in an extremely compact manner while Ab significantly affects the polymer conformation. The essentially larger hydrodynamic radii of conjugates, when compared with their radii of gyration, confirm the strong interaction of conjugates with solvent molecules.

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author
; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Macromolecular Bioscience
volume
1
issue
4
pages
7 pages
publisher
John Wiley & Sons Inc.
external identifiers
  • scopus:0038537751
ISSN
1616-5187
DOI
10.1002/1616-5195(20010601)1:4<157::AID-MABI157>3.0.CO;2-S
language
English
LU publication?
yes
id
7ff12893-a966-4ef6-b4e8-7e35b36e48de
date added to LUP
2022-05-13 10:47:20
date last changed
2022-05-13 10:47:20
@article{7ff12893-a966-4ef6-b4e8-7e35b36e48de,
  abstract     = {{<p>The effect of the conformational state of the polymer coil on the properties of protein-polymer conjugates has been studied for the conjugates of antibody (monoclonal antibody from 6C5 clone against inactivated rabbit muscle glyceraldehyde-3-phosphate dehydrogenase; Ab) with poly(methacrylic acid) (PMAA) or poly-(acrylic acid) (PAA). The pH-dependencies of molecular properties and structural parameters of aqueous solutions (radius of gyration, intensity of scattered light, hydrodynamic diameter, and polydisperisty index) of Ab, PMAA, and PAA, have been studied using static and dynamic light scattering techniques. While free Ab aggregates in solution and precipitates at its isoelectric point, the covalent attachment of a charged polymer to Ab prevents its association and shifts the precipitation point towards more acidic values (from pH 5.95 for Ab to pH ∼ 4.8 for Ab- PMAA). The predominant role of the conformational status of the polymer in the process of conjugate precipitation has been considered. Contrary to the precipitation of Ab-PMAA, the formation of stable colloidal particles was suggested for Ab-PAA at pH &lt; 4.8. In the conjugates, polymer chains surround the protein globule in an extremely compact manner while Ab significantly affects the polymer conformation. The essentially larger hydrodynamic radii of conjugates, when compared with their radii of gyration, confirm the strong interaction of conjugates with solvent molecules.</p>}},
  author       = {{Kazakov, Sergey V. and Muronetz, Vladimir I. and Dainiak, Maria B. and Izumrudov, Vladimir A. and Galaev, Igor Yu and Mattiasson, Bo}},
  issn         = {{1616-5187}},
  language     = {{eng}},
  month        = {{07}},
  number       = {{4}},
  pages        = {{157--163}},
  publisher    = {{John Wiley & Sons Inc.}},
  series       = {{Macromolecular Bioscience}},
  title        = {{Light Scattering Study of the Antibody-Poly(methacrylic acid) and Antibody-Poly(acrylic acid) Conjugates in Aqueous Solutions}},
  url          = {{http://dx.doi.org/10.1002/1616-5195(20010601)1:4<157::AID-MABI157>3.0.CO;2-S}},
  doi          = {{10.1002/1616-5195(20010601)1:4<157::AID-MABI157>3.0.CO;2-S}},
  volume       = {{1}},
  year         = {{2001}},
}