Ex Parte Nicolau

Patent Trial and Appeal Board

Feb 8, 2017

12424034 (P.T.A.B. Feb. 8, 2017)

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.
12/424,034 04/15/2009 Yves Claude NICOLAU 519865: SA9-002CON 9741
17387 7590 02/10/2017
Lathrop & Gage LLP/ Sanofi-Aventis
28 State Street
Boston, MA 02109
EXAMINER
BALLARD, KIMBERLY
ART UNIT PAPER NUMBER
1649
NOTIFICATION DATE DELIVERY MODE
02/10/2017 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):
bostonpatent @ lathropgage. com
PTOL-90A (Rev. 04/07)
UNITED STATES PATENT AND TRADEMARK OFFICE
BEFORE THE PATENT TRIAL AND APPEAL BOARD
Ex parte YVES CLAUDE NICOLAU1
Appeal 2014-008279
Application 12/424,034
Technology Center 1600
Before JOHN G. NEW, JAQUELINE T. HARLOW,
and TIMOTHY G. MAJORS, Administrative Patent Judges.
MAJORS, Administrative Patent Judge.
DECISION ON APPEAL
This is an appeal under 35 U.S.C. § 134 involving claims to a tetra-
palmitoylated beta-amyloid peptide, which have been rejected for non-
statutory obviousness-type double patenting. We have jurisdiction under
35 U.S.C. § 6(b).
We affirm.
STATEMENT OF THE CASE
Appellant’s “invention relates to the detection, treatment or
prevention of amyloidosis or amyloid-associated diseases.” (Spec. 1:12-14.)
1 Appellant identifies the Real Parties in Interest as Aventis Pharma S.S. and
Universite Louis Pasteur. (App. Br. 3.)
Appeal 2014-008279
Application 12/424,034
According to the Specification, “[a] number of impairments specific to
amyloid deposits in the brain are linked with the deposition of the peptide,
Ap peptide (amyloid-P peptide).” {Id. at 4.) Appellant discloses that such
impairments include Alzheimer’s Disease, among others. (Id.)
Claims 1, 3-13, and 17-20 are on appeal. Claim 1 is illustrative:
1. A tetra-palmitoylated beta-amyloid peptide having an N
terminus and a C terminus, wherein at least one of the
palmitoyl moieties is on a lysine residue forming a
palmitoylated lysine residue.
(App. Br. 12 (Claims App’x).)
The claims stand rejected on the grounds of nonstatutory obviousness-
type double patenting over claims 1-3, 5-7, 11-19, 22, 23, 37, 39, and 41 of
US 7,807,175 (“the ’175 patent”).
A hearing before the Board took place on January 19, 2017. (See
Hr’g Tr.)
DISCUSSION
Issue
Has the Examiner established by a preponderance of the evidence that
the rejected claims would have been obvious over claims 1-3, 5-7, 11-19,
22, 23, 37, 39, and 41 of the ’175 patent?
Findings of Fact (FF)
FF 1. Claim 1 of the ’175 patent recites
1. An antigenic construct comprising one or more copies of
Api-15 for the treatment of an amyloid associated disease or
condition,
2
Appeal 2014-008279
Application 12/424,034
wherein the A(3 peptide antigen is (a) pre-formed by on-
resin standard automated peptide synthesis and (b)
then modified by on-resin grafting of a lipophilic or
hydrophobic moiety to the terminal amino acid
residues of the pre-formed Ap peptide.
(’175 patent claim 1.)
FF 2. Claim 12 of the ’175 patent recites
12. An immunogenic composition comprising an Ap 1-15
peptide antigen for the treatment of an amyloid-associated
disease or condition,
wherein the Ap peptide antigen is (a) pre-formed by on-
resin standard automated peptide synthesis and (b)
then modified by on-resin grafting of a lipophilic or
hydrophobic moiety to the terminal amino acid
residues of the pre-formed Ap peptide, and
upon administration to an animal, including a human,
results mainly in the generation of antibodies of non­
inflammatory subtypes.
(Id. at claim 12.)
FF 3. Claim 22 of the ’175 patent recites
22. An immunogenic composition of claim 12 comprising an
immunogenic antigenic peptide for the treatment of an amyloid-
associated disease or condition, wherein the P-amyloid peptide
antigen is a palmitoylated Ap 1-15 peptide antigen modified by
between 2 and 4 covalently attached palmitoyl residues, at each
end of the peptide reconstituted in a liposome.
(Id. at claim 22; see also id. at claim 23.)
FF 4. The ’175 patent discloses “[f]or ACI-24 (b), two terminal
palmitoylated lysine residues were covalently linked at each end of Api-15
to reconstitute and anchor the antigen into liposome (a).” (Id. at 6:41 44;
see also id. at 42:30-38.) The ’175 patent further discloses:
3
Appeal 2014-008279
Application 12/424,034
It is a further object of the invention to provide a therapeutic
vaccine composition and a method of producing such a
composition using an immunogenic antigenic peptide . . .
especially a palmitoylated A(3 peptide fragment consisting of
amino acid residues 1-15 as given in SEQ ID NO: 1, and 1-
16(A14) as given in SEQ ID NO:3, modified by covalently
attachedpalmitoyl residues, particularly between 2 and 4
palmitoyl residues, more particularly 4 residues, coupled to
each terminus of the peptide antigen via one or more, but
particularly via one or two suitable amino acid residues such
as lysine, glutamic acid or cystein[e], or any other amino acid
residue that can be suitably used for coupling a palmitoyl
residue to the antigenic peptide.
{Id. at 11:44-12:15 (emphasis added); see also id. at 13:10-33.)
FF 5. The ’175 patent discloses, at Example 1, the “Synthesis of
Tetra(Palmitoyl Lysine)-ApMs Peptide Antigen.” (Id. at 40:30-36.) The
’175 patent discloses “Synthesis Protocol 1” for making the “palmitoylated
amyloid 1-15 peptide” that “involved on-resin grafting of palmitic acid to
the terminal Lys residues of the pre-formed peptide” and “Synthesis
Protocol 2,” which is “[a]n alternative approach [that] can be used for
synthesis of tetra(palmitoyl lysine)-APi-i5 peptide antigen based upon the
on-resin grafting of palmitic acid to the terminal Lysine residues of the pre­
formed peptide.” (Id. at 40:38^11-2.)
Principles of Law
Obviousness-type double patenting prohibits the issuance of claims in
a second patent that are “not patentably distinct from the claims of the first
patent.” In reLongi, 759 F.2d 887, 892 (Fed. Cir. 1985) (citations omitted).
“A later patent claim is not patentably distinct from an earlier patent claim if
the later claim is obvious over, or anticipated by, the earlier claim.” Eli Lilly
4
Appeal 2014-008279
Application 12/424,034
& Co. v. Barr Labs., Inc., 251F.3d955,968 (Fed. Cir. 2001) (citations
omitted).
In addressing a rejection for obviousness-type double patenting, we
ask: “Does any claim in the application define merely an obvious variation
of an invention disclosed and claimed in the patent? In considering the
question, the patent disclosure may not be used as prior art. This does not
mean that the disclosure may not be used at all. . . . [I]n certain instances it
may be used as a dictionary to learn the meaning of terms in a claim.” In re
Vogel, 422 F.2d 438, 441 (CCPA 1970) (citations omitted).
Analysis
Appellants do not argue the patentability of rejected claims 1, 3-13,
and 17-20 separately. We therefore select claim 1 as representative. 37
C.F.R. § 41.37(c)(l)(iv).
The Examiner finds that, “[ajlthough the claims at issue are not
identical, they are not patentably distinct from each other.” (Ans. 2.) More
specifically, the Examiner finds that at least claims 1,12, 22, and 23 of the
’175 patent
encompass a palmitoylated amyloid-P (Ap or beta-amyloid)
peptide, including those with between two and four covalently
attached palmitoyl residues at each end of the peptide (i.e., a
tetra-palmitoylated beta-amyloid), and which peptide is
reconstituted within a liposome and/or comprised within a
pharmaceutical composition with a carrier. In particular,
patented claims 22 and 23 [of the ’ 175 patent] are drawn to an
immunogenic composition comprising a palmitoylated Ap 1-15
peptide antigen that is modified by between 2 and 4 palmitoyl
residues covalently attached at each end of the peptide
reconstituted in a liposome.
5
Appeal 2014-008279
Application 12/424,034
(Id.) The Examiner finds, “[a]s a specific example of the immunogenic
peptide claimed by patented claims 22 and 23, Example 1 of the ’175 patent
. . . demonstrates a tetra(palmitoyl lysine)-A[31 -15 peptide.” (Id. at 2-3.)
Further, according to the Examiner, “the specification of the ’175 patent
indicates that palmitoyl residues are covalently coupled to each terminus of
the A(3 peptide via suitable amino acid residues, such as lysine.” (Id. at 3.)
The Examiner states that the ’175 specification has been considered
only to the extent necessary to support and define the invention claimed,
“such as defining how the palmitoyl residues are covalently attached to the
A(3 peptide.” (Id.) And the Examiner finds a “preferred embodiment of the
claimed invention comprises 4 palmitoyl residues added to the termini of the
A(3 peptide are palmitoyl lysine residues.” (Id.) Accordingly, the Examiner
concludes “the claims of the ‘175 patent render obvious the presently
claimed invention of a tetra-palmitoylated beta-amyloid peptide, wherein at
least one of the palmitoyl moieties is on a lysine residue forming a
palmitoylated lysine residue” as recited in pending claim 1. (Id.)
Appellant argues claims 1, 12, 22, and 232 of the ’175 patent “do not
encompass lysine linkers and the Examiner has not explained why a peptide
lacking lysine linkers would render a peptide with lysine linkers obvious.”
(App. Br. 5.) According to Appellant, “the specification . . . shows
embodiments of lipophilic or hydrophobic moieties being directly grafted to
2 Appellant contends that all the claims of the ’175 patent that are relied
upon for the double-patenting rejection “exclude the use of a lysine linker
with a palmitoyl residue” (App. Br. 5) but, like Appellant and the Examiner,
we focus on claims 1, 12, 22, and 23 of the ’175 patent.
6
Appeal 2014-008279
Application 12/424,034
an antigenic peptide without lysine linkers.” {Id. (emphasis added).)
Further, Appellant contends, “lysine linkers are not considered part of the
A(3 peptide nor are they lipophilic or hydrophobic moieties” based on the
way the respective linkers, peptide, and moieties are described or defined in
the ’175 patent’s specification. {Id. at 5-7.)
Appellant states that “the ‘175 patent teaches alternative embodiments
where palmitoyl groups are attached through amino acid linkers” but argues
that the portions of the ’175 patent that may be considered “are limited to
those teachings regarding binding of palmitoyl residues directly to the Api-
15 peptide.” {Id. at 8 (emphasis added).) According to Appellant, the
portions of the ’175 patent specification relied upon by the Examiner relate
to “embodiments [that] are not encompassed by the claims of the ‘175 patent
and . . . [t]hus, they are not available for use in this double patenting
rejection.” {Id. at 9.)
The Examiner has the better position.
As an initial matter, none of claims 1, 12, 22, or 23 recite the words
“direct” or “directly.” Nor does the specification of the ’175 patent use
those terms to describe the grafting of the hydrophobic or lipophilic moiety
to the peptide. Even if the claims might encompass a direct attachment —
e.g., with no intervening amino-acid linker or residue — between the
respective moieties and the A [3 peptide, the claims do not require it. And we
are unwilling to read limitations into the claims of the ’175 patent that would
exclude all but a direct attachment. Phillips v. AWH Corp., 415 F.3d 1303,
1320 (Fed. Cir. 2005) (“one of the cardinal sins of patent law—reading a
limitation from the written description into the claims”) (quoting SciMed
7
Appeal 2014-008279
Application 12/424,034
Life Sys., Inc. v. Advanced Cardiovascular Sys., Inc., 242 F.3d 1337, 1340
(Fed. Cir. 2001)).
Appellant directs us to portions of the ’175 patent’s specification that
Appellant contends teach “the binding of palmitoyl groups directly to the bl­
and C-termini of the Api-15 peptide.” (App. Br. 8 (citing ’175 patent
10:66-11:20, 12:32-61, and 25:51-26:16).) We agree with the Examiner,
however, that “the passages to which appellant refers are generic” and “in no
way preclude^ the presence of additional amino acids, such as linker
residues.” (Ans. 5-6.) As above, even if these passages support interpreting
the ’175 patent’s claims to encompass a direct grafting, they do not exclude
attachment through lysine residues. That is especially so when, as the
Examiner points out, “all of the exemplified liposomal vaccines [of the ’175
patent] comprising an A[3 peptide antigen include one or two lysine residues
at each termini of the Ap peptide.” (Ans. 6.)
Similarly, the language of the claims of the ’175 patent reciting “on-
resin grafting” does not imply only a direct grafting that excludes a lysine-
linker. The ’175 patent provides no special or express definition for that
phrase and Example 1 uses “on-resin grafting” to describe synthesis of
“Tetra(Palmitoyl Lysine)-Api-15 Peptide Antigen” — constructs that
include lysine residues. (FF 5.) If claims 1, 12, 22, and 23 were read in the
limited way urged by Appellant, the interpretation would be inconsistent
with the ’175 patent, which discloses on-resin grafting that expressly
encompasses attachment via lysine residues. We are thus not persuaded the
skilled artisan would understand the ’175 patent claims as excluding a lysine
residue or linker as alleged.
8
Appeal 2014-008279
Application 12/424,034
Contrary to Appellant’s arguments (App. Br. 8-10), the portions of
the ’175 patent specification considered by the Examiner were appropriate in
order to understand the bounds and interpret the scope of the patented claims
— particularly claim 22. Eli Lilly and Co. v. Leva Parenteral Medicines,
Inc., 689 F.3d 1368, 1378-79 (Fed. Cir. 2012) (describing the “general rule”
in obviousness-type double patenting determinations that “the earlier
patent’s written description [is] considered only to the extent necessary to
construe its claims.”). “The challenge of a double patenting analysis ... is
to understand the scope of the compared claims.” Geneva Pharms., Inc. v.
GlaxoSmithKline PLC, 349 F.3d 1373, 1385 (Fed. Cir. 2003) (holding that
where claim terms, standing alone, “do[] not adequately disclose the
patentable bounds of the invention[,]. . . [T]his court examines the
specifications of both [the earlier and later] patents to ascertain any overlap
in the claim scope for the double patenting comparison.”).
Claim 22 depends from claim 12 and recites, inter alia, “a
palmitoylated A [3 1-15 peptide antigen modified by between 2 and 4
covalently attached palmitoyl residues, at each end of the peptide.” (FF 3.)
The passages cited by the Examiner correspond specifically to how the ’175
patent covalently attaches between 2 to 4 palmitoyl residues to the Api-15
peptide as recited in claim 22. It is done through “suitable amino acid
residues such as lysine . . . that can suitably be used for coupling a palmitoyl
residue to the antigenic peptide.” (FF 4.) These disclosures are not merely
described as “alternative embodiments” as Appellant suggests; rather, they
are introduced in the ’ 175 patent as “a further object of the invention” and as
“[a]lso part of the invention.” (FF 4; ’175 patent 11:44 and 13:10.) These
9
Appeal 2014-008279
Application 12/424,034
disclosures thus support claim 22 and were properly invoked by the
Examiner to aid in defining the claim’s full scope.3 (Ans. 7.)
In further support, the Examiner finds that there are “no actual
showings or demonstrated examples in the ‘ 175 patent of antigenic
constructs comprising a lipophilic or hydrophobic moiety directly grafted
onto an A(3 peptide without use of a lysine residue.” (Ans. 6.)
Appellant does not dispute the Examiner’s finding and, instead,
“submit[s] that this is inapposite to the scope of claims 1 and 12 of the ‘175
patent.” (Reply Br. 3.) Per Appellant, “[according to the definitions of the
terms used in claims 1 and 12 of the ‘ 175 patent, the claims exclude the
examples provided in specification.” {Id.)
Appellant’s argument is not persuasive. In effect, Appellant advances
an interpretation of ’ 175 patent’s claims that would exclude every working
example described in the specification. On the record before us, such an
interpretation is not reasonable. See generally Vitronics Corp. v.
Conceptronic, Inc., 90 F.3d 1576, 1583 (Fed. Cir. 1996) (“Indeed, if‘solder
reflow temperature’ were defined to mean liquidus temperature, a preferred
(and indeed only) embodiment in the specification would not fall within the
scope of the patent claim. Such an interpretation is rarely, if ever, correct
and would require highly persuasive evidentiary support, which is wholly
3 Claim 23 depends from claim 22. Because claim 22 depends from claim
12, claim 12 is broader than, and encompasses, claim 22’s scope. Claims 1
and 12 of the ’175 patent are similar with respect to the limitations relevant
to this appeal. {See FF 1-2.)
10
Appeal 2014-008279
Application 12/424,034
absent in this case.”); Johns Hopkins Univ. v. Cellpro Inc., 152 F.3d 1342,
1355 (Fed. Cir. 1998).
Appellant has not presented persuasive evidentiary support for its
narrow interpretation of the ’175 patent’s claims. Even assuming the A (3
peptide and the hydrophobic or lipophilic moiety are defined in the manner
suggested by Appellant (App. Br. 5-7, Reply Br. 3—4), the claims of the
’175 patent do not require a direct grafting of the moiety to the peptide that
excludes a lysine residue or linker as discussed above. Moreover, as
conceded by Appellant, all of the ’175 patent’s examples are to the contrary
— palmitoyl residues are connected to the peptide through lysine residues.
(Ans. 6; Reply Br. 3.) This is not a matter of the Examiner “improperly
importing limitations” into the claims as Appellant alleges. (Reply Br. 3.)
An interpretation that encompasses — but is not necessarily limited to — the
’175 patent’s examples is more reflective of the ordinary and customary
meaning of the claims to the skilled artisan at the time of invention.
For these reasons, we agree with the Examiner that claim 1 in the
pending application defines an obvious variation of the invention of claims
1, 12, 22, and 23 in the ’175 patent.
Conclusion of Law
We conclude the Examiner established by a preponderance of the
evidence that pending claim 1 would have been obvious over claims 1-3, 5-
7, 11-19, 22, 23, 37, 39, and 41 of the ’175 patent. Claims 3-13, and 17-20
have not been argued separately and thus fall with pending claim 1.
11
Appeal 2014-008279
Application 12/424,034
SUMMARY
We affirm the rejection of claims 1,3-13, and 17-20 on the grounds
of nonstatutory obviousness-type double patenting over claims 1-3, 5-7, 11-
19, 22, 23, 37, 39, and 41 of the ’175 patent.
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
12