Ex Parte Schenk

Board of Patent Appeals and Interferences

Feb 18, 2011

10923469 (B.P.A.I. Feb. 18, 2011)

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.
10/923,469 08/20/2004 Dale B. Schenk 057437-391869 8115
826 7590 02/22/2011
ALSTON & BIRD LLP
BANK OF AMERICA PLAZA
101 SOUTH TRYON STREET, SUITE 4000
CHARLOTTE, NC 28280-4000
EXAMINER
KOLKER, DANIEL E
ART UNIT PAPER NUMBER
1649
MAIL DATE DELIVERY MODE
02/22/2011 PAPER
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.
PTOL-90A (Rev. 04/07)
UNITED STATES PATENT AND TRADEMARK OFFICE
__________

BEFORE THE BOARD OF PATENT APPEALS
AND INTERFERENCES
__________

Ex parte DALE B. SCHENK
__________

Appeal 2010-004538
Application 10/923,469
Technology Center 1600
__________

Before ERIC GRIMES, JEFFREY N. FREDMAN, and STEPHEN
WALSH, Administrative Patent Judges.

GRIMES, Administrative Patent Judge.

DECISION ON APPEAL1
This is an appeal under 35 U.S.C. § 134 involving claims to a method
of treating Alzheimer’s disease. The Examiner has rejected the claims for

1 The two-month time period for filing an appeal or commencing a civil
action, as recited in 37 C.F.R. § 1.304, or for filing a request for rehearing,
as recited in 37 C.F.R. § 41.52, begins to run from the “MAIL DATE”
(paper delivery mode) or the “NOTIFICATION DATE” (electronic delivery
mode) shown on the PTOL-90A cover letter attached to this decision.
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anticipation, obviousness, and (provisionally) for obviousness-type double
patenting. We have jurisdiction under 35 U.S.C. § 6(b). We affirm-in-part.
STATEMENT OF THE CASE
The Specification discloses that Alzheimer's disease “is characterized
by at least two types of lesions in the brain, senile plaques and
neurofibrillary tangles” (Spec. 1, ¶ 0003). The Specification also discloses
that “[t]he principal constituent of the [senile] plaques is a peptide termed
Aβ or β-amyloid peptide” (id. at ¶ 0004).
Claims 164, 166, 168, 177-184, 187, 188, 190-201, 203-206, 210-217,
220, 221, and 223-226 are on appeal. Claims 164 and 197 are representative
and read as follows:
164. A method of treating Alzheimer’s disease, comprising
administering to a patient in need thereof an effective amount of a
humanized antibody that binds to soluble Aβ and specifically binds to an
epitope having an amino acid between positions 10-25.

197. A method of treating Alzheimer’s disease, comprising
administering to a patient in need thereof an effective amount of a
humanized antibody that specifically binds to dissociated Aβ without
binding to aggregated Aβ.

The claims stand rejected as follows:
• Claims 197, 210-217, 220, and 223-226 under 35 U.S.C. § 102(b) in
view of Becker;2
• Claim 164, 166, 168, 177-184, 187, 190-201, 203-206, 210-217,
220, and 223-226 under 35 U.S.C. § 103(a) in view of Becker, Solomon,3
and Nordstedt;4

2 Becker et al., EP 0 613 007, Aug. 31, 1994
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• Claim 164, 166, 168, 177-184, 187, 188, 190-201, 203-206, 210-
217, 220, 221, and 223-226 under 35 U.S.C. § 103(a) in view of Becker,
Solomon, Nordstedt, and Plückthun;5 and
• Claims 164, 166, 168, 177-184, 187, 188, 190-198, 200, 201, 203-
206, 210-217, 220, 221, and 223-226 for obviousness-type double patenting
in view of claims 1, 2, 4, 6-8, 10-12, 17, 21-25, 27, 31, 32, 35-37, 56-58, 60-
67, 69-74 and 76-78 of Application 09/322,289.
I.
Issue
The Examiner has rejected claims 197, 210-217, 220, and 223-226
under 35 U.S.C. § 102(b) as anticipated by Becker. The claims have not
been argued separately and therefore stand or fall together. 37 C.F.R.
§ 41.37(c)(1)(vii).
The Examiner finds that Becker discloses the “treatment of
Alzheimer’s disease by administration of antibodies” (Answer 4). The
Examiner further finds that Becker discloses “two specific types of
antibodies, those that bind to the β-amyloid peptide … in β-sheet
conformation without substantially binding to [the] α-helical form…, as well
as antibodies that bind to the α-helical form without substantially binding to

3 Beka Solomon et al., Monoclonal antibodies inhibit in vitro fibrillar
aggregation of the Alzheimer β-amyloid peptide, 93 PROC. NATL. ACAD. SCI.
USA 452-455 (1996).
4 Nordstedt et al., WO 97/21728, June 19, 1997.
5 Andreas Plückthun, Mono- and Bivalent Antibody Fragments Produced in
Escherichia coli: Engineering, Folding and Antigen Binding, 130
IMMUNOLOGICAL REVIEWS, 151-188 (1992).
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the β-sheet form” (id.). The Examiner further finds that Becker discloses
that “the term ‘antibody’ includes humanized antibodies” (id. at 5).
Appellant contends that Becker only discusses the therapeutic and
diagnostic uses for the disclosed antibodies generally, and it is unclear which
of the two types of antibodies is intended for therapeutic use (Appeal Br. 11-
12).
The issue with respect to this rejection is: Does the evidence of
record support the Examiner’s finding that Becker discloses treating
Alzheimer’s disease with antibodies that bind to dissociated Aβ without
binding to aggregated Aβ, as recited in claim 197?
Findings of Fact
1. Becker discloses antibodies that “demonstrate specificity for
β-amyloid peptides which are predominantly β-sheet in conformation.…
These antibodies show little binding specificity for β-amyloid peptides
which have a great deal of random coil and/or a-[sic, α-]helix in the
secondary structure.” (Becker col. 7, ll. 26-32.)
2. Becker also discloses “antibodies which are specific for β-amyloid
peptides which have adopted a random coil or α-helix conformation. These
antibodies show little binding specificity for β-amyloid peptides which have
a great deal of β-sheet conformation.” (Id. at col. 7, ll. 33-38.)
3. Becker discloses that
[t]hese antibodies are used in diagnostics, therapeutics or in
diagnostic/therapeutic combinations.… By ‘therapeutics’ and
‘therapeutic/diagnostic combinations’ as used herein is
respectively meant the treatment or the diagnosis and treatment
of disease states or biological status via the in vivo
administration to mammals, preferably humans, of the
antibodies of the present invention. The antibodies of the
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present invention are especially preferred in the diagnosis
and/or treatment of Alzheimer’s disease in mammals,
preferably humans.
(Id. at col. 7, ll. 39-44.)
4. Becker discloses that its use of the term “antibody” includes
humanized antibodies (id. at col. 5, ll. 51-58).
Analysis
Claim 197 is directed to a method of treating Alzheimer’s disease,
comprising administering to a patient an effective amount of a humanized
antibody that specifically binds to dissociated Aβ without binding to
aggregated Aβ.
Becker discloses antibodies, including humanized antibodies (FF 4),
that bind specifically to β-amyloid peptides in either the β-sheet or α-helix
conformation (FFs 1, 2). As Appellant has pointed out, Aβ in the β-sheet
conformation is aggregated and Aβ in the random coil conformation is
monomeric (Appeal Br. 10). Thus, Becker’s antibodies that bind
specifically to Aβ in the random coil conformation meet the limitation of
binding specifically to dissociated Aβ but not to aggregated Aβ. Becker also
discloses that “[t]hese antibodies” are used in “treatment of Alzheimer’s
disease in mammals, preferably humans” (FF 3).
Appellant contends that Becker is unclear whether it is the antibody
that binds the β-sheet form of β-amyloid or the antibody that binds the
random coil form of β-amyloid that is intended for therapeutic use (Appeal
Br. 11-12). Thus, Appellant argues that Becker’s referral “to multiple
classes of antibodies and multiple utilities with the disjunctive term ‘or’
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creates an ambiguity as to which class of antibody is intended for which
utility” (id. at 12).
Appellant’s argument is not persuasive. Becker discloses two types of
antibodies, and states that “[t]hese antibodies” are useful for therapy,
without distinguishing between the two types of Aβ-binding antibodies.
Thus, the most reasonable interpretation of Becker is that it discloses using
either of the two types of antibodies in Alzheimer’s disease therapy.
Appellant also argues that Becker discloses “the β-sheet form of Aβ is
associated with toxicity” and thus it would suggest using the antibodies that
bind to the β-sheet form for therapeutic use, rather than the antibodies that
bind to the random coil form (Reply Br. 3-4).
This argument is also unpersuasive. Although Becker provides more
explanation of why the antibodies that bind the β-sheet conformation of Aβ
are expected to be useful in therapy, as compared to the antibodies that bind
to the random coil conformation, it nonetheless describes the two types of
antibodies (FFs 1, 2) and immediately follows those descriptions with its
statement that “[t]hese antibodies” are used for “diagnosis and/or treatment
of Alzheimer’s disease” (FF 3), without distinguishing which antibodies are
used which way. As discussed above, the most reasonable interpretation of
Becker’s disclosure is that it describes either of the two types of antibodies
as being useful in diagnosis and in therapy.
Conclusion of Law
The evidence of record supports the Examiner’s finding that Becker
discloses treating Alzheimer’s disease with antibodies that bind to
dissociated Aβ without binding to aggregated Aβ, as recited in claim 197.
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II.
Issue
The Examiner has rejected claims 164, 166, 168, 177-184, 187, 190-
201, 203-206, 210-217, 220, and 223-226 under 35 U.S.C. § 103(a) in view
of Becker, Solomon, and Nordstedt.
The Examiner relies on Becker as discussed above. The Examiner
finds that Solomon discloses “antibodies which bind to aggregating epitopes
of Aβ, i.e. those regions within the protein which induce formation of fibrils
or aggregates,” and their use in treating Alzheimer’s disease (Answer 6).
The Examiner finds that Nordstedt discloses “that the sequence ‘KLVFF’,
which corresponds to residues 16-20 of Aβ … is required for the
polymerization, or aggregation, of Aβ protein and subsequent formation of
fibrils” and “compounds which bind to this sequence should be used to
inhibit polymerization of Aβ peptide … for treatment of Alzheimer’s
disease” (id.). The Examiner concludes that it would have been obvious to
one of ordinary skill in the art to modify Becker’s Alzheimer’s treatment
method “by using antibodies that bind to residues 16-20, as suggested by
Solomon and Nordstedt” (id.) because “Solomon teaches antibodies against
aggregating epitopes should be used, and Nordstedt specifically teaches that
residues 16-20 constitute such an aggregating epitope” (id.).
Appellant contends that the references do not provide a reasonable
expectation of success for the claimed method (Appeal Br. 15-17, 19-21)
and the art as a whole did not point to amino acids 16-20 of Aβ “as being the
key region to focus therapeutic treatments” (id. at 17).
The issues with respect to this rejection are: Does the evidence of
record support the Examiner’s conclusions that the cited references would
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have suggested residues 16-20 of Aβ as a target for therapeutic treatment
and would have provided a reasonable expectation of success for the method
of claim 164?
Additional Findings of Fact
5. Solomon discloses that “β-amyloid peptide, the hallmark of
Alzheimer’s disease, forms fibrillar toxic aggregates in brain tissue”
(Solomon, abstract).
6. Solomon discloses monoclonal antibodies “raised against
β-amyloid fragments spanning amino acid residues 1-28 and 8-17 of the
β-amyloid peptide chain” (id.).
7. Solomon discloses that the “mAbs prevent the [in vitro]
aggregation of β-amyloid peptide and … the inhibitory effect appears to be
related to the localization of the antibody binding sites and the nature of the
aggregating agents” (id.).
8. Solomon discloses that the “[p]reparation of mAbs against
‘aggregating epitopes,’ defined as sequences related to the sites where
protein aggregation is initiated, may lead to the … prevention of protein
aggregation” (id.).
9. Solomon discloses that its results “may provide a foundation for
using mAbs in vivo to prevent the β-amyloid peptide aggregation that is
associated with Alzheimer disease” (id.).
10. Nordstedt discloses that “the polymerization of the amyloid β
peptide (Aβ) into amyloid fibrils is a critical step in the pathogenesis of
Alzheimer’s disease” (Nordstedt 3: 14-16).
11. Nordstedt discloses that “Aβ molecules interact with a high
degree of specificity during polymerization and fibril formation. It was
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assumed that ligands which bind to recognition sequences would be capable
of inhibiting Aβ polymerization.” (Id. at 3: 17-26.)
12. Nordstedt discloses that “the Lys-Leu-Val-Phe-Phe (KLVFF)
sequence in Aβ is necessary for polymerization to occur. Peptides
incorporating this sequence bind to Aβ and are capable of blocking the fibril
formation of Aβ-1-40 and are therefore potentially useful as drugs” (id. at
3: 32-37).
13. Nordstedt discloses that the KLVFF sequence corresponds to
amino acids 16-20 of Aβ (id. at 4: 9-10).
14. Nordstedt discloses “the use of a compound … which is able to
bind to the KLVFF-sequence in amyloid β peptide and which has the ability
to inhibit polymerization of amyloid β peptide, for the manufacture of a
medicament for … the treatment or prevention of Alzheimer’s disease” (id.
at 8: 12-19).
Analysis
We have found that claim 197 is anticipated by Becker. Thus we
affirm the rejection of claim 197 as being obvious in view of Becker,
Solomon and Nordstedt. “It is well settled that ‘anticipation is the epitome
of obviousness.’” In re McDaniel, 293 F.3d 1379, 1385 (Fed. Cir. 2002).
Claims 198-201, 203-206, 210-217, 220, 223, and 224 fall with claim 197.
37 C.F.R. § 41.37(c)(1)(vii)
Claim 164 is directed to a method of treating Alzheimer’s disease by
administering a humanized antibody that binds to soluble Aβ at an epitope
between amino acids 10 and 25.
Solomon discloses that antibodies binding to Aβ within amino acids
1-28 or 8-17 prevent aggregation of the peptide, and suggests that antibodies
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that bind to aggregating epitopes may be useful in preventing the Aβ
aggregation seen in Alzheimer’s disease patients. Nordstedt discloses that
ligands that bind the sequence KLVFF (amino acids 16-20 of Aβ) prevent
Aβ aggregation. Nordstedt suggests that KLVFF-binding compounds would
be useful for treating Alzheimer’s disease. Becker discloses treating
Alzheimer’s disease using antibodies that bind to the Aβ peptide. We agree
with the Examiner that, in view of these teachings, it would have been
obvious to treat Alzheimer’s disease using antibodies that bind to amino
acids 16-20 of the Aβ peptide.
Appellant argues that the cited references do not provide a reasonable
expectation of success for the claimed method (Appeal Br. 15-17, 19-21).
Appellant cites news reports as evidence that researchers regarded the
success of an immunization approach in slowing or preventing the
development of β-amyloid plaques in a mouse Alzheimer’s model as being
dramatic and surprising (id. at 15-17).
Appellant’s argument is not persuasive. As Appellant concedes,
“these comments were made primarily with reference to active
immunotherapy rather than passive immunotherapy as claimed” (Appeal Br.
16). That is, the reports addressed an approach of administering Aβ peptides
to generate an immune response, not administering antibodies directly. As
one of the reports states, “[a]lmost all scientists would have dismissed the
immunization approach … because of the ‘dogma’ that the so-called blood-
brain barrier keeps circulating antibodies out of the brain” (Travis, 156
SCIENCE NEWS ONLINE 2 (July 10, 1999)). That is, those skilled in the art
doubted that antibodies in the bloodstream would be able to cross the blood-
brain barrier and reach the brain.
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As recognized by the Examiner, however, the claims are not limited to
methods of administration that require the antibody to cross the blood-brain
barrier but encompass “any route of administration” (Answer 13). Becker
teaches that antibodies can be “administered by infusion” (Becker, col. 8,
l. 40), which would have reasonably suggested direct infusion to the brain or
cerebral spinal fluid, in view of the prevailing view that the blood-brain
barrier keeps circulating antibodies out of the brain. Walker,6 cited by
Appellant, provides additional evidence that this route of administration
would have been obvious, in its disclosure that “a monoclonal antibody
infused into the cerebrospinal fluid (CSF) of aged monkeys is capable of
binding selectively to Aβ deposits in the living brain.” (Walker 377, right
col.).
Appellant also argues that the cited art as a whole did not point amino
acids 16-20 of Aβ “as being the key region to focus therapeutic treatments”
(Appeal Br. 17). Appellant argues that Roberts7 “teaches away from the
notion that residues 16-20 are an effective anti-aggregating epitope” because
that peptide “had no effect in a mouse model of Alzheimer's disease…,
whereas certain other peptides had memory enhancing effects” (Appeal Br.
17-18).
The Examiner responds that Roberts’ disclosure that a peptide
“consisting of residues 16 - 20 of Aβ, is not therapeutic” in an animal model
of Alzheimer’s disease “does not show that antibodies against residues 16-

6 Lary C. Walker et al., Labeling of Cerebral Amyloid In Vivo with a
Monoclonal Antibody, 53 J. NEUROPATHOL. EXP. NEUROL. 377-383 (1994)
7 Roberts, WO 95/08999, April 6, 1995.
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20 would be ineffective” (Answer 12). We agree with the Examiner’s
reasoning and conclusion.
Appellant also argues that references other than those cited by the
Examiner taught that regions other than amino acids 16-20 of Aβ were
important for β sheet formation (Appeal Br. 18) and “pointed to regions
other than 16-20 of Aβ as having a role in aggregation or otherwise
mediating toxicity” (id.). Appellant concludes that “[a]lthough not all these
references negate Aβ16-20 as having a possible role in aggregation, they do
teach away from it being the only such epitope or the critical epitope for
therapeutic efficacy and set the artisan on a divergent path from the claimed
methods” (id. at 19).
This argument is not persuasive. The references cited by the
Examiner disclose that Aβ polymerization is a critical step in Alzheimer’s
disease pathogenesis and that amino acids 16-20 of Aβ are necessary for
polymerization (FFs 10, 12, 13); suggest preventing aggregation using
antibodies that bind “aggregating epitopes” (FF 8); and disclose that
antibodies that bind Aβ can be used to treat Alzheimer’s disease (FF 3). The
Examiner’s references therefore would have led those of ordinary skill in the
art to amino acids 16-20 as a target for antibodies used for treating
Alzheimer’s disease. The fact that other parts of Aβ were considered
promising targets for Alzheimer’s disease treatments does not cast doubt on
the suggestion of the Examiner’s references to target amino acids 16-20.
We also disagree that the references cited by Appellant teach away
from the claimed methods. While the cited references may suggest other
approaches for mitigating the role of Aβ protein in the pathological process,
they do not provide reason for expecting that inhibiting Aβ aggregation
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using antibodies that bind aggregating epitopes would not be successful. See
In re Gurley, 27 F.3d 551, 553 (Fed. Cir. 1994) (“[I]n general, a reference
will teach away if it suggests that the line of development flowing from the
reference’s disclosure is unlikely to be productive of the result sought by the
applicant.”).
For the reasons discussed above, we affirm the rejection of claim 164
as being obvious in view of Becker, Solomon and Nordstedt. Claims 166,
168, 177-184, 187, 190, and 191 fall with claim 164 because Appellant did
not provide separate reasons for their patentability. 37 C.F.R.
§ 41.37(c)(1)(vii).
With respect to claims 192-196, 225, and 226 Appellant argues that
the cited references do not suggest the claimed methods because these
claims require the peripheral administration of the antibody (Reply Br. 8).
We agree with Appellant that the Examiner has not adequately
explained how the cited references would have suggested, with a reasonable
expectation of success, the peripheral administration of an antibody for the
treatment of Alzheimer’s disease. As discussed above, the evidence of
record shows that those of ordinary skill in the art would have expected the
blood-brain barrier to prevent peripherally administered antibodies from
reaching the brain.
The Examiner’s reasoning (Answer 13) that Becker teaches
intravenous administration is not persuasive. Becker teaches that antibodies
“can be dissolved in one of the commonly used intravenous fluids and
administered by infusion” (Becker, col. 8, ll. 39-40). “[D]issolv[ing] in
intravenous fluid,” however, is not the same as intravenous administration.
In view of the evidence of record showing that those skilled in the art knew
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the effect of the blood-brain barrier, the Examiner has not adequately
explained why the cited passage would have been read as disclosing
peripheral administration. Thus, the rejection of claims 192-196, 225 and
226 as being obvious in view of Becker, Solomon, and Nordstedt is
reversed.
Conclusion of Law
The evidence of record supports the Examiner’s conclusions that the
cited references would have suggested residues 16-20 of Aβ as a target for
therapeutic treatment and would have provided a reasonable expectation of
success for the method of claim 164. However, the evidence of record does
not support the Examiner’s conclusion that the cited references would have
suggested peripheral administration of antibodies to treat Alzheimer’s
disease.
III
The Examiner has rejected claims 164, 166, 168, 177-184, 187, 188,
190-201, 203-206, 210-217, 220, 221, and 223-226 under 35 U.S.C.
§ 103(a) in view of Becker, Solomon, Nordstedt, and Plückthun. The
Examiner concludes that Plückthun would have made obvious the additional
limitation of claims 188 and 221 (Answer 7). We agree with the Examiner’s
findings and conclusion.
Appellant does not dispute that Plückthun would have made obvious
the additional limitation of claims 188 and 221, but argues that Plückthun
does not cure the deficiencies of Becker, Solomon, and Nordstedt with
regard to independent claim 164 (Appeal Br. 26).
With respect to claim 164, this argument is not persuasive for the
reasons discussed above. Claims 166, 168, 177-184, 187, 188, 190, 191,
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197-201, 203-206, 210-217, 220, 221, 223, and 224 fall with claim 164. 37
C.F.R. § 41.37(c)(1)(vii).
However, the Examiner has not adequately explained how Plückthun
would have made up for the deficiency of Becker, Solomon, and Nordstedt,
as discussed above, in suggesting claims 192-196, 225, and 226. Thus, we
reverse the rejection of those claims.
IV.
The Examiner has provisionally rejected claims 164, 166, 168, 177-
198, 200, 201, 203-206, 210-217, 220, 221, and 223-226 for obviousness-
type double patenting on the basis that they are not patentably distinct from
some of the claims of Application No. 09/322,289 (Answer 3-4). The
Examiner finds that “[m]any of the claims in the ‘289 application … are
generic with respect to the epitope to which the administered antibody will
bind” (id. at 4), but the “specification of the ‘289 application clearly
indicates that the applicant in that case … considered antibodies that bind to
an epitope having an amino acid between positions 10-25, 10-20, or 15-20 of
Aβ as part of his invention” (id.).
Appellant contends that the rejection places “impermissible reliance
on the specification of the cited application. …[N]o genuine issue of claim
construction requiring resort to the specification has been identified”
(Appeal Br. 9).
We agree with Appellant that the Examiner has not adequately
explained how claims on appeal define an obvious variant of the cited claims
of the ‘289 application. The claims on appeal require either an “antibody
that specifically binds to dissociated Aβ without binding to aggregated Aβ”
(claim 197) or one that “specifically binds to an epitope having an amino
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acid between positions 10-25” (claim 164). The Examiner has not pointed to
any claims of the ‘289 application that require either of these properties, but
relies on the specification of the ‘289 application to suggest them.
However, while an application’s specification can be relied on to
interpret a claim term or to understand the meaning of a claim, see MPEP
§ 804(II)(B)(1), it cannot be used as though it were prior art if it does not
otherwise qualify as such. General Foods Corp. v. Studiengesellschaft
Kohle mbH, 972 F.2d 1272, 1279 (Fed. Cir. 1992). Thus, the double
patenting rejection is reversed.
SUMMARY
We affirm the rejection of claims 197, 210-217, 220, and 223-226
under 35 U.S.C. § 102(b) and the rejection of claims 164, 166, 168, 177-184,
187, 188, 190, 191, 197-201, 203-206, 210-217, 220, 221, 223, and 224
under 35 U.S.C. § 103(a).
However, we reverse the rejection for provisional double patenting
and the rejection of claims 192-196, 225, and 226 under 35 U.S.C. § 103(a).
TIME PERIOD FOR RESPONSE
No time period for taking any subsequent action in connection with
this appeal may be extended under 37 C.F.R. § 1.136(a).

AFFIRMED-IN-PART

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