Stephen M. Strittmatter

Patent Trials and Appeals Board

Oct 30, 2019

14272874 - (D) (P.T.A.B. Oct. 30, 2019)

UNITED STATES PATENT AND TRADEMARK OFFICE
UNITED STATES DEPARTMENT OF COMMERCE
United States Patent and Trademark Office
Address: COMMISSIONER FOR PATENTS
P.O. Box 1450
Alexandria, Virginia 22313-1450
www.uspto.gov
APPLICATION NO. FILING DATE FIRST NAMED INVENTOR ATTORNEY DOCKET NO. CONFIRMATION NO.
14/272,874 05/08/2014 Stephen M. Strittmatter 047162-5157US1(00238) 4983
78905 7590 10/30/2019
Saul Ewing Arnstein & Lehr LLP (Philadelphia)
Attn: Patent Docket Clerk
Centre Square West
1500 Market Street, 38th Floor
Philadelphia, PA 19102-2186
EXAMINER
CHONG, YONG SOO
ART UNIT PAPER NUMBER
1627
NOTIFICATION DATE DELIVERY MODE
10/30/2019 ELECTRONIC
Please find below and/or attached an Office communication concerning this application or proceeding.
The time period for reply, if any, is set in the attached communication.
Notice of the Office communication was sent electronically on above-indicated "Notification Date" to the
following e-mail address(es):
patents@saul.com
PTOL-90A (Rev. 04/07)
UNITED STATES PATENT AND TRADEMARK OFFICE
__________

BEFORE THE PATENT TRIAL AND APPEAL BOARD
__________

Ex parte STEPHEN M. STRITTMATER

__________

Appeal 2018-004447
Application 14/272,874
Technology Center 1600
__________

Before ULRIKE W. JENKS, TIMOTHY G. MAJORS, and
MICHAEL A. VALEK, Administrative Patent Judges.

MAJORS, Administrative Patent Judge.

DECISION ON APPEAL
Appellant1 submits this appeal under 35 U.S.C. § 134 involving
claims to a method of treating an Aβ-modulated disease, including
Alzheimer’s Disease, in a mammal. The Examiner rejected the claims as
obvious. We have jurisdiction under 35 U.S.C. § 6(b).
We REVERSE.

1 Appellant identifies the Real Party in Interest as Yale University and
AstraZeneca AB. Appeal Br. 2.
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STATEMENT OF THE CASE
“Alzheimer’s Disease (AD) is the most common dementing illness
and afflicts over 5 million people in the USA currently, with an annual
health care burden near $ 200 billion.” Spec. 1:17–19. “[C]linical dementia
of AD is coupled with a distinct pathology, with senile plaques consisting of
amyloid-β (Aβ) peptide, and with neurofibrillary tangles consisting of
hyperphosphorylated Tau protein.” Id. at 1:20–22.
The Specification explains that “[l]arge extracellular and inert plaques
of amyloid mark the pathology, but attention has focused on
conformationally distinct soluble oligomers of Aβ (Aβo) as being
neurotoxic,” which neurotoxicity is characterized by synaptic malfunction
and loss of dendritic spines. Id. at 2:5–10. Such synaptic changes are,
according to the Specification, “followed by neurofibrillary tangles, neuro-
inflammation, and neuronal cell loss.” Id. at 2:10–11.
In a genome-wide screen for Aβo binding sites, the prion protein
(PrPc) was identified. Id. at 2:13–14. The Specification explains that PrPc is
Aβo specific, with little or no affinity for fibrillary or monomeric states. Id.
at 2:13–15. According to the Specification, “the ability of human AD brain-
derived Aβ species to suppress hippocampal synaptic plasticity requires
PrPc, and human AD contains PrPc-interacting Aβo species and Aβ-PrPc
complexes.” Id. at 2:26–28.
The Specification discloses that, in most trials, the approach to
treating AD has “centered on efforts to alter Aβ itself (e.g., its production or
clearance or aggregation).” Id. at 3:2–3. According to the Specification,
“[n]o major trial has centered on the signal transduction downstream of toxic
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Aβ species,” and “there has been no successful clinical trial targeting Tau
and/or Tau kinases in AD to this date.” Id. at 3:3–5.
Various enzymes of the Src family of tyrosine kinases are expressed
in the central nervous system, with Src and Fyn being the mostly highly
expressed members of that family in the brain. Id. at 3:6–8. Activity of
these enzymes, the Specification explains, is regulated by intramolecular
interactions that depend on an equilibrium between tyrosine phosphorylation
and dephosphorylation. Id. at 3:8–10. With regard to Fyn, in particular, the
Specification describes Fyn’s localization to the post-synaptic density
fraction of the brain, and Fyn’s regulation of glutamate2 receptor trafficking
and synaptic plasticity. Id. at 3:17–18. This regulation occurs via Fyn’s
phosphorylation of the NMDA-type glutamate receptor subunits, NR2A and
NR2B. Id. at 3:21–22.
The Specification describes “experiments demonstrating that
oligomers of Aβ bound to PrPc activate Fyn to damage neurons in AD.” Id.
at 8:10–12 (“Figure 1A: Aβo increases NR2B phosphorylation via PrPc and
Fyn.”); see also id. at Fig. 1E (experiments showing lost/retracted dendritic
spines following exposure to Aβo), Fig. 1F (showing model of the dendritic
spine, wherein Aβo binds to PrPc and causes Fyn activation and, via
phosphorylation of the NR2B subunit, NMDA receptor redistribution in the
cell—resulting in excitotoxicity, spine retraction, and network dysfunction),
8:21–26, 53:3–11. The Specification further describes “experiments

2 Glutamate is a major excitatory neurotransmitter. Spec. 3:17.
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demonstrating that saracatinib inhibits Fyn and [the] Aβo-induced signaling
in neurons.” Id. at 8:29–30, Figs. 2A–2D.
Appellant’s “invention provides a pharmaceutical composition
comprising an effective amount of saracatinib” and, more specifically, “a
method of treating or preventing an Aβ-modulated disease or disorder in a
mammal in need thereof” via “administering to the mammal a
therapeutically effective amount of [saracatinib as] a Fyn inhibitor.” Id. at
3:27–4:3.
Claims 11–13, 18–22, 24–32, 37–41, and 43–49 are on appeal.
Independent claim 11 is representative, and reads:
11. A method of treating an Aβ-modulated disease or
disorder in a mammal in need thereof, the method
comprising administering to the mammal a therapeutically
effective amount of saracatinib, or a pharmaceutically
acceptable salt thereof, wherein the free concentration of
saracatinib in the plasma of the mammal ranges from
about 2.6 to about 41.2 nM.

Appeal Br. 16 (Claims App’x).
The other independent claim, claim 31, is similar to claim 11, but
recites a “method of minimizing or reversing loss of cognition in a mammal
in need thereof,” and further requires “administering . . . a therapeutically
effective amount of saracatinib, or a pharmaceutically acceptable salt
thereof, wherein the free concentration of saracatinib in the plasma of the
mammal ranges from about 2.6 to about 41.2 nM.” Id. at 17–18. Illustrative
dependent claims include the following: claim 12 recites that the Aβ-
modulated disease is, for example, Alzheimer’s Disease; and claim 26
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recites administering at least one additional agent (in addition to saracatinib)
that treats or prevents the Aβ-modulated disease or disorder in the mammal.
The claims stand rejected under 35 U.S.C. § 103(a) as obvious over
Settembre,3 Ford,4 and Hrakovsky.5 See Final Act. 4–6; Ans. 3–8.
DISCUSSION
The issue on appeal is whether a preponderance of the evidence cited
by the Examiner supports the Examiner’s conclusion of obviousness.
The Examiner concludes that each of the claims on appeal would have
been obvious over Settembre, Ford, and Hrakovsky. Final Act. 4–6. The
Examiner finds that Settembre “teach[es] a method of treating Alzheimer’s
disease by administering to a subject a therapeutically effective amount of an
inhibitor (claims 36, 38, 40) belonging to the family of Src kinases (claims
23–24), for example, saracatinib (page 47).” Id. at 4. The Examiner finds,
however, that Settembre “fail[s] to specifically disclose the claimed dosages
and administration techniques as well as another active agent [as required in
certain dependent claims, such as claim 26].” Id. The Examiner, thus, turns
to Ford and Hrakovsky.
According to the Examiner, Ford teaches AZD0530 difumarate (a salt
of saracatinib),6 and pharmaceutical compositions including this compound
for oral, topical, parenteral, and other routes of administration. Final Act. 4.
The Examiner finds that, for oral administration, Ford teaches 0.5–500 mg

3 Settembre et al., WO 2012/120048 A1, published Sept. 13, 2012.
4 Ford et al., US 8,304,417 B2, issued Nov. 6, 2012.
5 Hrakovsky et al., US 2008/0008752 A1, published Jan. 10, 2008.
6 See Spec. 13:5–10.
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of the active agent, especially 125–225 mg, may be used. Final Act. 4; see
Ford 21:47–61 (describing use for treatment of cancer).
The Examiner cites Hrakovsky as teaching that the agent
“memantine” is approved for treatment of AD. Final Act. 5 (citing
Hrakovsky ¶ 4).
The Examiner notes that “[a]ny properties exhibited by or benefits
from [a chemical composition] are not given any patentable weight over the
prior art,” reasoning that such properties are “inherent” and that a “chemical
composition and its properties are inseparable.” Final Act. 5.
The Examiner concludes it would have been obvious “to orally
administer saracatinib difumarate in the claimed dosages in combination
with memantine for the treatment of Alzheimer’s disease in a subject in need
thereof.” Id. According to the Examiner, one would have been motivated to
administer AZD0530 difumarate because Ford teaches such agent is
sufficiently stable and may be prepared in high yield. Id. Moreover, the
Examiner notes, Hrakovsky teaches that another agent, memantine, is safe
and effective for AD treatment. Id. Hence, the Examiner reasons, the
ordinarily skilled person would have “a reasonable expectation of success in
treating Alzheimer’s disease . . . by administering a composition comprising
saracatinib difumarate and memantine for their therapeutically additive
effect.” Id. at 5–6.
Appellant raises several arguments in response. First, Appellant
argues that Settembre, considered as a whole, teaches away from a selection
of saracatinib for treatment of AD and, specifically, cuts against the notion
of using the substantially-lower levels of saracatinib for treating AD that are
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recited in the claims. According to Appellant, Settembre requires its
compounds inhibit TFEB phosphorylation and mobilize cytosolic TFEB to
the nucleus7 as the basis for its purported treatment of some 70-plus distinct
diseases. Id. at 5–7. Appellant contends Settembre teaches that saracatinib,
at best, had only “modest activity” in mobilizing TFEB to the nucleus—with
an EC50 falling somewhere between 7,000–15,000 nM. Id. at 4–5; see also
generally Settembre 27–48 (identifying saracatinib as a category “B”
compound, and contrasting with potent category “A” compounds, such as
Torin1 and Torin2). Hence, Appellant argues, the ordinarily skilled person
would have understood that much greater concentrations (e.g., in the range
of 7–15 μM) than what is recited in the pending claims would have been
required to provide the activity desired and described in Settembre. Appeal
Br. 4–5 (noting that the concentration recited in the claims “ranges from
about 2.6 to about 41.2 nM — that is at least 3 orders of magnitude

7 Appellant’s reading of Settembre appears to be correct insofar as Settembre
describes and claims a mechanism of action requiring inhibition of TFEB
phosphorylation as a means of mobilizing cytosolic TFEB to the nucleus,
and thus activating lysosomal biogenesis. See generally Settembre 1–2,
claims 1, 2, 27, 36, 37. Settembre discloses that “transcription factor EB
(TFEB)” is a master gene for lysosomal biogenesis, driving expression of
both autophagy and lysosomal genes. Settembre 2:1–5; see also id. at 2:6–
12 (“applicants found that nuclear localization and activity of TFEB are
regulated by specific serine phosphorylations . . . [and] inhibition of specific
phosphorylation induces autophagy by activating TFEB”), 2:13–15
(“applicants found that pharmacological inhibition of TFEB phosphorylation
can be used in vivo to activate the lysosomal and autophagic system of the
cells and thus it represents a tool to treat different pathologic conditions”),
2:18–20 (“pharmacological inhibition [of the phosphorylation of TFEB] . . .
activates TFEB by promoting its nuclear translocation”).
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(1,000 times) lower than the concentrations taught in Settembre”).
According to Appellant, even if Settembre could be credibly read as
suggesting the use of saracatinib to treat AD, the “disclosure in Settembre
indicates that the presently claimed circulating levels of saracatinib (from
about 2.6 to about 41.2 nM) would not be useful in treating AD.” Appeal
Br. 5 (“[O]ne skilled in the art would not have had a reasonable
expectation at all that the present methods [of the claims] would be useful
for treating AD.”).
Second, Appellant contends the Examiner’s rejection does not meet
the obviousness criteria specified in the Supreme Court’s KSR decision.
Appeal Br. 5–10. According to Appellant, none of the applied art teaches or
suggests all the elements of the claimed methods, particularly the recited
range of free plasma concentration ranging from about 2.6 to about 41.2 nM
as providing a therapeutically effective treatment for an Aβ-modulated
disease. Id. at 7. Moreover, Appellant argues, Settembre “provides no
actual data indicating that any TFE[B] phosphorylation inhibitor, let alone
any Src kinase, let alone saracatinib specifically, can be used to treat AD.”
Id. at 7–8 (contending that Settembre lists numerous A, B, and C compounds
in a Table, but provides no data to show any treatment of AD as one of “76
wholly distinct diseases” identified in Settembre). Appellant contends that
one skilled in the art would not have selected saracatinib out of the many
compounds listed in Table 4, given its “B”-level activity. Id. at 8. And,
even if saracatinib was selected, Appellant argues the Examiner has not
demonstrated that the ordinarily skilled person would have been motivated
to treat AD with the respectively lower concentrations (i.e., 1000-times
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lower) of saracatinib recited in the claims with a reasonable expectation of
success that such dosages/concentrations would provide effective AD
treatment. Id. at 8–9, 13–14.
Third, Appellant argues that the invention provides unexpected
results. Appeal Br. 9–14. Specifically, Appellant contends evidence shows
that the claimed method provides surprisingly efficacious treatment of an
Aβ-modulated disease without significant side effects. Id. Citing pages 55–
57 of the Specification and Kaufman,8 Appellant contends the data shows
that treatment of mice with the presently claimed method9 “unexpectedly
modifies the pathology associated with AD, reversing memory deficits and
restoring synaptic density.” Appeal Br. 9–10.
Moreover, Appellant argues, the claimed treatments are provided with
minimal to no side effects. Id. at 10–12. Citing the Specification, Appellant
contends toxicology studies on dogs and a dosing study on 24 human
subjects revealed no significant safety concerns or adverse events and, in

8 Adam C. Kaufman et al., Fyn Inhibition Rescues Established Memory and
Synapse Loss in Alzheimer Mice, 77:6 Annals of Neurology 953–971 (2015).
9 As Appellant notes, the Specification and Kaufman also describe a phase
Ib dose study on humans with mild to moderate AD, where the patients were
dosed up to 125mg/day, providing a trough CSF concentration of 2.5–14.0
nM, which closely correlates to saracatinib CSF levels between mice and
humans. Appeal Br. 10; Spec. 58–59; Kaufman 957–959. The Specification
further correlates CSF levels to plasma levels, with a low-end plasma
concentration range of about 2.6–6.5 nM (with 50mg of saracatinib) and a
high end range of about 7.4–41.2 nM (with 125mg of saracatinib). Spec.
58:4–14, Figs. 6, 8–9.
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particular, “no significant hematological changes.”10 Id. at 12 (Appellant
contends Kaufman (pg. 963) corroborates the lack of chronic toxicity with
treatment of AD using saracatinib). Appellant argues the observed lack of
significant side effects stands in contrast to the reported adverse events with
saracatinib administration to cancer patients. Citing the “AZD0530 Cancer
Label,” which is of record, Appellant identifies the adverse events observed
including nausea, vomiting, and diarrhea, as well as “haematological
changes” observed in toxicity studies. Appeal Br. 11. Appellant also cites a
published study by Gucalp11 relating to a Phase II trial of saracatinib in
patients with a form of metastatic breast cancer. Id. Appellant contends
Gucalp evidences that patients receiving a 175 mg daily dose of saracatinib
showed no complete or partial cancer response, or stable disease at six
months, and that the observed adverse events included elevated liver
chemistries, nausea, and adrenal insufficiency, among others. Id.; see also
Gucalp Abst. (“The majority . . . of patients discontinued saracatinib because
of disease progression. . . . Common adverse events included fatigue,

10 The Specification reports that, in the dog studies, “[t]here were no obvious
adverse symptoms at 8.75 months, and the continued weight gain of dogs
receiving the saracatinib (Figure 7) suggests that there are no unexpected
safety concerns with chronic use.” Spec. 58:8–10. In the human study,
“[t]here were no apparent study-related serious adverse events (SAEs),
significant laboratory abnormalities, or early terminations. In particular,
there were no significant hematological changes.” Id. at 58:19–21.
11 Ayca Gucalp et al., Phase II trial of saracatinib (AZD0530), an oral src-
inhibitor for the treatment of patients with hormone receptor negative
metastatic breast cancer, NIH-PA Author Manuscript 1–12 (2011).
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elevated liver chemistries, nausea, hyponatremia, dyspnea, cough, and
adrenal insufficiency.”).
The Examiner “bears the initial burden . . . of presenting a prima facie
case of unpatentability.” In re Oetiker, 977 F.2d 1443, 1445 (Fed. Cir.
1992). “The Patent Office has the initial duty of supplying the factual basis
for its rejection. It may not . . . resort to speculation, unfounded assumptions
or hindsight reconstruction to supply deficiencies” in the cited references. In
re Warner, 379 F.2d 1011, 1017 (CCPA 1967). Upon considering the
applied prior art, and the argument and evidence of record for and against
the rejection, we are not persuaded the Examiner has met the burden to show
that the pending claims would have been obvious.
At the outset, we note and agree with Appellant’s observation that
Settembre provides little to no detail or data about how lysosomal
biogenesis, via activation of TFEB, purports to treat all of the widely diverse
diseases it lists, much less how that mechanism of action would treat AD in
particular. Appeal Br. 5–8; see generally Settembre 4–5 (listing, for
example, lysosomal storage diseases including Danon disease, Krabbe
disease, hepatic diseases such as Fatty liver disease, muscle diseases such as
Autophagic Vacuolar Myopathies, and neurodegenerative diseases including
Alzheimer’s disease, Parkinson’s disease, and Huntington’s disease, among
others).12 Nor does Settembre provide details about the specific amounts of

12 Insofar as Settembre broadly discloses controlling, at the transcriptional
level, the lysosomal-autophagic pathway as potentially modulating cellular
clearance of toxic molecules, we note that this contrasts with the mechanism
of action behind Appellant’s invention, which targets downstream
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saracatinib (listed as one of several structurally and functionally distinct
compounds in Table 4) that would actually be required to provide a
therapeutically effective treatment to any such disease or condition, much
less AD, in a subject. See Settembre 28–48 (Table 4). And, the Examiner
provides no evidence or persuasive technical reasoning to support a
determination that the therapeutically effective treatment of AD, with the
varied compounds like those disclosed in Settembre, is considered
predictable among skilled persons.
That being said, even if, by virtue of picking and choosing from
among the diverse compounds and diseases listed in Settembre, we agreed
that the skilled person would have chosen saracatinib for the treatment of
AD, we cannot disregard that Settembre’s disclosed method of action
requires TFEB activation and mobilization of TFEB to the nucleus. Indeed,
the claims of Settembre that the Examiner strings together in making the
rejection depend (directly or indirectly) from claims 1 and 2, which
expressly recite that the compounds are for inhibiting TFEB
phosphorylation. See, e.g., Settembre, claim 2 (“The inhibitor of TFEB
phosphorylation according to claim 1 acting on a kinase of the pathway of
the TFEB phosphorylation.”); see generally id. at Abstr., 1–4. The only
cited information in Settembre about the use of saracatinib for that method is
that saracatinib has only moderate activity, with an EC50 of greater than

intracellular signaling of Aβo as distinct from approaches aimed at Aβ
clearance itself. See supra 2–3.
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7,000 nM, and possibly as high as 15,000 nM.13 Settembre 28:3–6 (“‘B’
means the compound has an EC50 of greater than 7000 but less than or
equal to 15000”), 46–47 (identifying saracatinib in a tenth family of
compounds, and having an EC50 of “B”).
We are unable to conclude, on this record, that the ordinarily skilled
person would have predictably decreased those concentrations in Settembre
by several orders of magnitude, believing that such a decrease would have
been effective in inhibiting TFEB phosphorylation and mobilization of
TFEB to the nucleus for lysosomal biogenesis, much less that such a
decrease would have been therapeutically effective in treating AD. Put
differently, we ask whether the ordinarily skilled person, considering
Settembre, would have had a reasonable expectation that decreasing the
disclosed concentration of >7,000 nM to, say, 7 nM (within the respectively
narrow range of Appellant’s claims) would successfully provide a
therapeutically effective treatment to AD as claimed? On this record, we
think not.
The Examiner initially responds that Appellant’s arguments on these
points are unpersuasive “because the free concentration of saracatinib in the
plasma is primarily determined by the actual dosage amounts.” Final Act. 8.

13 We recognize Settembre’s cited testing is a cellular assay, testing a variety
of compounds (one of which was saracatinib) for their in vitro effectiveness
as kinase inhibitors that induce mobilization of cystosolic TFEB to the
nucleus, and not a test of actual and effective concentrations of the active in
an in vivo setting. See Settembre 27:9–28:9. But that only underscores the
prophetic nature of Settembre’s disclosure with respect to saracatinib and
whether it might possibly provide an effective treatment for the 70-plus
diverse diseases listed, or AD in particular.
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As we understand the Examiner’s position, because Ford discloses a dosage
range of a saracatinib salt for oral administration (e.g., 125–225mg) that
overlaps with amounts of dosages recited in certain of the pending
dependent claims (e.g. claim 29, reciting a daily dose of about 50, 100, or
125 mg), some of Ford’s dosages would provide plasma concentrations in
mammals within the scope of the claims. Id.
Even if there is overlap when Ford’s dosages are factored in, the
Examiner’s position is, however, unpersuasive. First, as Appellant notes, the
Examiner’s position is not responsive to the argument advanced by
Appellant—seeking evidence-backed reasons to explain why the skilled
artisan would have used far lower concentrations than are arguably
suggested in Settembre with a reasonable expectation of providing effective
AD treatment. Appeal Br. 5. Second, while true that Ford discloses dosages
that partly overlap with the dosages appearing in some of Appellant’s
claims, Ford uses saracatinib solely to treat cancers. Ford 1:24–48
(disclosing AZD0530 as “a selective inhibitor of the motility of tumour cells
and a selective inhibitor of the dissemination and invasiveness of
mammalian cancer cells leading to inhibition of metastatic tumour growth”),
22:5–27, 22:39–50. The Examiner provides no persuasive reasoning or
evidence to explain why Ford’s treatment of cancer with the allegedly
overlapping amounts of saracatinib salts would have provided a reasonable
expectation that such amounts would successfully treat Alzheimer’s Disease,
or other Aβ-modulated diseases or disorders.
The Examiner offers a new argument on this issue in the Answer.
According to the Examiner, there is no standard that requires the dosage be
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at or above a compound’s EC50 amount, which reflects a concentration
where 50% of the maximum effect is observed. Ans. 4. Invoking a
description about dose-response curves from Wikipedia, the Examiner
suggests that a desired effect may arise at amounts slightly greater than a
drug’s threshold dose with side effects becoming more pronounced at higher
doses. Id. Accordingly, the Examiner states that one would not start with
Settembre’s EC50 concentration, but “much lower” where the curve is above
zero or above a threshold-dose to avoid side effects. Id.
On this record, we do not find Examiner’s position persuasive. The
Examiner’s position is wanting for sufficient evidentiary support. On such a
critical point in view of the arguments here, we decline to treat Wikipedia as
authoritative. The Examiner cites no persuasive evidence to support the
notion that the ordinarily skilled person designing pharmaceuticals and
methods of treatment of the type claimed would, as of routine, simply start
with dosages at a point “where the [dose-response] curve is above zero.”
There is no persuasive evidence cited to suggest what the Examiner’s
alleged “threshold dose” of saracatinib would be able to provide Settembre’s
method of activating TFEB at a level that it might effectively treat AD,
much less that it would be close to or within the concentrations recited in the
claims. The appropriate dosages for mammals likely turns on a complex
interplay of pharmacokinetic and pharmacodynamic activity of saracatinib
necessary to achieve the inhibiting effect, and TFEB nuclear mobilization
that Settembre aims to induce. Based on such variables, the amount needed
to provide effective treatment, as judged by Settembre, may be higher or
lower than the observed EC50 amounts. We do not know based on the
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evidence here. But, given the record as it is, we agree with Appellant that
there is no sufficient showing that the skilled artisan would have a
reasonable expectation of success in treating AD with saracatinib
concentrations as low as recited in the claims for the reasons explained
above.
Having determined that the preponderance of the evidence does not
demonstrate the claims would have been prima facie obvious over
Settembre, Ford, and Hrakovsky, we decline to reach Appellant’s argument
on alleged unexpected results.
CONCLUSION
For the reasons explained above, we find the preponderance of the
evidence cited by the Examiner does not support the Examiner’s conclusion
that claims 11–13, 18–22, 24–32, 37–41, and 43–49 would have been
obvious over Settembre, Ford, and Hrakovsky.
DECISION SUMMARY
In summary:
Claim(s)
Rejected
35 U.S.C.
§
Reference(s)/Basis Affirmed Reversed
11–13, 18–
22, 24–32,
37–41, 43–
49
103 Settembre, Ford,
Hrakovsky
11–13, 18–
22, 24–32,
37–41, 43–
49

REVERSED