Appeal 2007-0856
Application 09/281,474
and a biological-function domain” that is “conformationally constrained
upon complexing the metal ion-binding backbone with the metal ion”
(Sharma, col. 10, ll. 8-15). The biological-function domain “may constitute
a ligand capable of forming a member of a ligand and receptor pair” (id. at
col. 10, ll. 45-48). The metal ion acts as a label (id. at col. 1, ll. 22-23). In
particular, Sharma describes “a molecule which, upon complexing with a
metal ion, includes a biological-function domain which is specific for one or
more of the RGD-binding integrin family of receptors for use in diagnostics
and therapeutic modalities” (id. at col. 20, ll. 17-21).
In addition, Sharma describes a metal ion-binding backbone including
a plurality of amino acids having nitrogen, sulfur, or oxygen atoms available
to complex the metal ion (id. at col. 10, ll. 28-35). The preferred backbone
is “based on the requisite number of particular coordinating groups required
by the coordination sphere of a given complexing metal ion” (id. at col. 27,
ll. 12-15). “Coordinating groups in the peptide chain include nitrogen atoms
of amine, [or] amide . . . ; [and] sulfur atoms of thiols” (id. at col. 27, ll. 21-
23). Specifically, Sharma describes a tetradentate peptide construct of, e.g.,
N3S or N2S2 (id. at col. 27, ll. 30-42). Based on the teachings of Sharma, we
agree with the Examiner that it would have been obvious to include a
diaminedithiol, a monoamine-monoamidedithiol, a triamide-monothiol, or a
monoamine-diamide-monothiol as the metal binding domain of Palladino.
With regard to claim 1, Palladino discloses that the labels may be
“attached by spacer arms of various lengths to reduce potential stearic [sic,
steric] hindrance” (Palladino, col. 6, ll. 54-55). In addition, Sharma depicts
a metallopeptide having a C(=O) between the metal ion-binding backbone
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