Barbara Hribar (Author)

Abstract

The aggregation propensity of monoclonal antibodies can be modified by adding different cosolutes into the solution. A simple coarse-grained model in the combination with the thermodynamic perturbation theory was used to predict cluster distribution and viscosity of the solutions of IgG4 monoclonal anibody in the presence of L-Arginine Hydrochloride. The data were analysed using binding polynomial to describe the binding of cosolute (Arginine) to the antibody molecule. The results show that by binding to the antibody molecule the cosolute occupies some of the binding sites of the antibody, and in this way reduces the amount of binding sites available to other antibody molecules. The aggregation propensity of the antibody molecules is therefore reduced.

Keywords

monoklonska protitelesa;agregacija;viskoznost;sotopljenci;termodinamska perturbacijska teorija;statistična vsota vezanja;monoclonal antibody;aggregation;viscosity;cosolutes;thermodynamic perturbation theory;binding polynomial;

Data

Language: English
Year of publishing:
Typology: 1.01 - Original Scientific Article
Organization: UL FKKT - Faculty of Chemistry and Chemical Technology
UDC: 544.35:577.322
COBISS: 121626627 Link will open in a new window
ISSN: 0167-7322
Views: 73
Downloads: 32
Average score: 0 (0 votes)
Metadata: JSON JSON-RDF JSON-LD TURTLE N-TRIPLES XML RDFA MICRODATA DC-XML DC-RDF RDF

Other data

Secondary language: Slovenian
Secondary keywords: monoklonska protitelesa;agregacija;viskoznost;sotopljenci;termodinamska perturbacijska teorija;statistična vsota vezanja;
Type (COBISS): Article
Pages: str. 1-5
Issue: ǂVol. ǂ366
Chronology: 15 Nov. 2022
DOI: 10.1016/j.molliq.2022.120349
ID: 17188702