Barbara Hribar (Avtor)

Povzetek

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.

Ključne besede

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

Podatki

Jezik: Angleški jezik
Leto izida:
Tipologija: 1.01 - Izvirni znanstveni članek
Organizacija: UL FKKT - Fakulteta za kemijo in kemijsko tehnologijo
UDK: 544.35:577.322
COBISS: 121626627 Povezava se bo odprla v novem oknu
ISSN: 0167-7322
Št. ogledov: 73
Št. prenosov: 32
Ocena: 0 (0 glasov)
Metapodatki: JSON JSON-RDF JSON-LD TURTLE N-TRIPLES XML RDFA MICRODATA DC-XML DC-RDF RDF

Ostali podatki

Sekundarni jezik: Slovenski jezik
Sekundarne ključne besede: monoklonska protitelesa;agregacija;viskoznost;sotopljenci;termodinamska perturbacijska teorija;statistična vsota vezanja;
Vrsta dela (COBISS): Članek v reviji
Strani: str. 1-5
Zvezek: ǂVol. ǂ366
Čas izdaje: 15 Nov. 2022
DOI: 10.1016/j.molliq.2022.120349
ID: 17188702