Appeal 2007-0856
Application 09/281,474
combination” and that N2S2 is the “same as [claim 53’s] diaminedithiol or
monoamine-monoamidedithiol combination” (id. at 11). The Examiner also
argues that Sharma discloses “a peptide chain linked to a N3S containing
chelator by a C(=O) spacer group” (id.).
The Examiner concludes that “one of ordinary skill in the art would be
motivated to combine the teachings of Palladino et al and Sharma et al since
both references are directed to peptides that may be labeled and contain a
linking group” (id. at 10). “[W]hile Appellant[s] assert[] that the complexes
of Sharma et al are conformationally constrained, the pending claims do not
exclude conformationally constrained conjugates” (id.).
We conclude that the Examiner has set forth a prima facie case that
claims 1, 52, and 53 would have been obvious. With regard to claim 52,
Palladino describes a non-RGD peptide that binds to the αvβ3 integrin
receptor and the use of this peptide for treating or detecting diseases
involving this receptor (Palladino, col. 7, ll. 13-28). To diagnose disease,
Palladino describes “determining the level of binding of the peptide to the
αvβ3 integrin receptor. . . . To determine the level of binding, the peptide is
labelled with a detectable label” (id. at col. 19, l. 61, to col. 20, l. 19). As a
label, Palladino describes “polypeptide epitopes recognized by a secondary
reporter,” for example, “metal binding domains” (id. at col. 6, ll. 37-54).
Based on the teachings of Palladino, we conclude that it would have been
obvious to combine a metal binding domain, which constitutes a chelator as
this term is used in the Specification, with the non-RGD peptide.
With regard to claim 53, Sharma describes a metallo-construct
including “a metal ion-binding backbone for complexing with a metal ion,
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