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Updated: Dec 10, 2025

Determination of the Relative Potency of an Anti-TNF Monoclonal Antibody mAb by Neutralizing TNF Using an In Vitro Bioanalytical Method
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The structure of myeloid cell-specific TNF inhibitors affects their biological properties

Ekaterina A Vasilenko1, Ekaterina N Gorshkova1, Irina V Astrakhantseva1,2

  • 1Lobachevsky State University, Nizhny Novgorod, Russia.

FEBS Letters
|September 1, 2020
PubMed

Spatial organization and conformational changes of antibodies may significantly affect their biological functions. We assessed the effect of mutual organization of the two VH H domains within bispecific antibodies recognizing human TNF and the surface molecules of murine myeloid cells (F4/80 or CD11b) on TNF retention and inhibition. TNF-neutralizing properties in vitro and in vivo of MYSTI-2 and MYSTI-3 antibodies were compared with new variants with interchanged VH H domains and different linker sequences. The most effective structure of MYSTI-2 and MYSTI-3 proteins required the Ser/Gly-containing 'superflexible' linker. The orientation of the modules was crucial for the activity of the proteins, but not for MYSTI-3 with the Pro/Gln-containing 'semi-rigid' linker. Our results may contribute toward the development of more effective drug prototypes.

Keywords:
VHHanti-TNF therapybispecific antibodieslinkers

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