Appeal No. 1997-4379
Application No. 08/278,437
selective in its inhibitory actions. This evidence taken together with other findings,
suggests heterogeneity in receptor type. Since it is fundamental that the structure of a
peptide, i.e., amino acid order and chemical linkages, is what determines its function,
the ordinarily skilled worker would have recognized that the different structures of the
claimed cyclic peptides would have precluded any expectations about how they would
behave" (Examiner's Answer, page 6). Mather's discloses the use of an octreotide, a
synthetic analog of somatostatin, as an inhibitor (abstract). Mather specifically
discloses that "some of [the octreotides] are in the (D) configuration in order to enhance
the stability of the molecule in vivo" (id.). The main purpose of using this analog is to
increase the half-life to avoid rapid secretion by the liver and the kidney experienced by
the somatostatin which "severely limited [its] therapeutic application" (Mather, page 94).
At best, Mather teaches that adopting a specific configuration (conformation) can
increase the stability of analogs while retaining its bioactivity. We fail to see how the
examiner's position with respect to Mather serves as evidence that appellants'
modification of the disulfide bond destroys the bioactivity of the peptide.
According to the examiner, Rivier "states that '... potency is decreased as a
result of the loss of groups which are important either to maintaining the conformation
of the molecule or to the binding and activation of the receptor ... thus, there appear to
be strict structural requirements for high potency ...'" (id.). The examiner's position,
however, does not take into account that appellants' invention does not lead to "loss of
groups." What appellants' invention does is modify an existing disulfide bond so as to
maintain the conformation and bioactivity of the peptide. Again, we fail to see how the
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