Appeal 2007-0856
Application 09/281,474
angiogenic-based diseases (Answer 5). The Examiner argues that Palladino
describes “non-RGD (RGD is the peptide sequence Arg-Gly-Asp) peptides
that bind to the αvβ3 integrin receptor” (id.). The Examiner also argues that
Palladino discloses that the “peptides may be labeled and discloses that a
metal binding domain[] may be utilized. . . . [T]he phrase ‘metal binding
domains’ is equivalent to ‘chelators’ in the art.” (Id. at 9-10.) In addition,
the Examiner argues that Palladino “disclose[s] that the labels are optionally
attached by spacer arms of various lengths to reduce potential stearic [sic,
steric] hindrance. . . . [T]he phrase ‘spacer’ is interchangeable with . . .
‘linking group’ in the art.” (Id. at 10.)
The Examiner relies on Sharma for disclosing “peptide
metalloconstructs that are useful for biological, therapeutic, diagnostic
imaging, or radiotherapeutic purposes” (id. at 6). The Examiner argues that
Sharma “is directed to peptides that . . . may be cyclic RGD mimics . . . ,
which are complexed with a metal ion binding backbone (chelator) and
complexed with a metal” (id. at 10). The Examiner also argues that Sharma
discloses that the peptide (i.e., the biological-function domain) is “distinct”
from the metal binding backbone (id. at 7).
In addition, the Examiner argues that Sharma discloses “[v]arious
chelators/ligands containing nitrogen, oxygen, and sulfur based coordination
atoms . . . used to generate a tetradentate peptide construct. The tetradentate
structure may be N4, N3S, N2S2, NS3, N2SO, or any similar combination
yielding tetradentate coordination utilizing nitrogen, sulfur, and oxygen
atoms.” (Id.) In particular, the Examiner argues that N3S is the “same as
[claim 53’s] triami[d]e-monothiol or monoamine-diamide-monothiol
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