Biomedical Engineering Reference
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FIGURE 38.3 Formation of CovX-Body using 1,3-diketone based linker and structures of
representative small molecule pharmacophores with 1,3-diketone linkers that were used to generate
selective and potent CovX-Bodies targeting CCR5, endothelin A, and a v b 3 integrin receptors.
precedence in other commercial therapeutic antibodies, such
as Synagis 1 and Erbitux 1 . The resulting humanized version
of 38C2 referred to as CVX-2000, was stably transfected
into Chinese hamster ovary cells, and serves as the common
carrier scaffold for all CovX-Bodies in preclinical and
clinical development. It is 98.2% human when compared
to murine 38C2 antibody. Only 12 of the 667 light and heavy
chain amino acids in CVX-2000 are retained from the
murine sequence: seven in the heavy chain (out of 448),
and five in the light chain (out of 219). On the basis of the 3D
structure, all five of the light chain murine-sequence residues
are buried (core) residues, and therefore unlikely to be of
immunogenic potential. Four of the seven heavy chain
retained murine residues are buried as well. Of the three
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