Abstract
Spatial organization and conformational changes of antibodies maysignificantly affecttheir biological functions. We assessedthe 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 requiredthe Ser/Gly-containing 'superflexible' linker. The orientation of the modules was crucial fortheactivity oftheproteins, but not for MYSTI-3 with the Pro/Gln-containing 'semi-rigid' linker. Our resultsmay contribute toward the developmentof more effective drug prototypes.
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