immatics biotechnologies GmbH

Patent Trials and Appeals Board

Oct 27, 2020

15226126 - (D) (P.T.A.B. Oct. 27, 2020)

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.
15/226,126 08/02/2016 Toni WEINSCHENK 2912919-018008 3220
84331 7590 10/27/2020
McBee Moore & Vanik, IP, LLC
7900 Westpark Drive, Suite A100
McLean, VA 22102
EXAMINER
RAWLINGS, STEPHEN L
ART UNIT PAPER NUMBER
1643
NOTIFICATION DATE DELIVERY MODE
10/27/2020 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):
docketing@mmviplaw.com
eofficeaction@appcoll.com
smcbee@mmviplaw.com
PTOL-90A (Rev. 04/07)
UNITED STATES PATENT AND TRADEMARK OFFICE
__________

BEFORE THE PATENT TRIAL AND APPEAL BOARD
__________

Ex parte TONI WEINSCHENK, OLIVER SCHOOR,
CLAUDIA TRAUTWEIN, NORBERT HILF,
STEFFEN WALTER, and HARPREET SINGH
__________

Appeal 2020-000111
Application1 15/226,126
Technology Center 1600
__________

Before RICHARD M. LEBOVITZ, RYAN H. FLAX, and
RACHEL H. TOWNSEND, Administrative Patent Judges.

TOWNSEND, Administrative Patent Judge.

DECISION ON APPEAL
This is an appeal under 35 U.S.C. § 134(a) involving claims to a
pharmaceutically acceptable salt of a particular peptide sequence, and a
fusion protein, which have been rejected as directed to patent-ineligible
subject matter, and/or as being indefinite and for obviousness-type double
patenting. We have jurisdiction under 35 U.S.C. § 6(b).

1 We use the word “Appellant” to refer to “applicant” as defined in
37 C.F.R. § 1.42. Appellant identifies the real party in interest as Immatics
Biotechnologies GmbH. (Appeal Br. 1.)
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We reverse the rejection for patent-ineligible subject matter, but
affirm the obviousness-type double patenting rejection which was not
challenged on appeal.
STATEMENT OF THE CASE
Claims 1–4, 7, 9–14, and 21–27 are on appeal. Claim 1 is
representative and reads as follows:
1. A peptide consisting of the amino acid sequence of
GLWHHQTEV (SEQ ID NO: 21) in the form of a
pharmaceutically acceptable salt, wherein said peptide is
produced by solid phase peptide synthesis or produced by a
yeast cell or bacterial cell expression system.
(Appeal Br. 48.)

The following grounds of rejection by the Examiner are before us on
review:
Claims 1, 3, 4, 9–14, and 21–26 under 35 U.S.C. § 101 as being
directed to patent-ineligible subject matter.2
Claims 1, 3, 4, 9–14, and 21–27 on the ground of nonstatutory
obviousness-type double patenting as being unpatentable over claims 1–16
of U.S. Patent No. 9,289,478.

2 In the Final Rejection the Examiner rejected claims 1–4, 7, 9–14, and 21–
26. In the Answer, the Examiner withdrew the rejection as applied to claims
2 and 7. The Examiner also withdrew the rejection of claims 2 and 7 under
35 U.S.C. §112(b) as being indefinite.
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DISCUSSION
I
I. Patent Eligible Subject Matter
The Dispute
The Examiner finds that claim 1 is directed to a judicial exception,
“namely, a peptide or a composition comprising a peptide in which the
peptide is not markedly different from a naturally occurring peptide, such
that claimed invention is distinguished from the naturally occurring
product.” (Final Action 2–3, 7.) The Examiner states:
the derivation of a salt of the peptide does not create a marked
difference between the claimed invention and the naturally
occurring peptide. This is especially true since upon
dissolution of the salt the peptide [] is present in solution as it
exists in nature. Similarly it is submitted that the acylation or
pegylation of the peptide or its linkage to a solid resin does not
substantially alter its structure by creating a marked and
significant difference between it and its naturally occurring
counterpart.
(Id. at 3.) The Examiner indicates that formation of a salt, or acylating a
peptide, may be analogized to putting a scarf around a snowman, in that the
addition of the scarf does not change the structure of the underlying
snowman. (Id. at 9–10.) The Examiner indicates that just as the snowman
structure is the same when the scarf is removed, the removal of the salt
group from the peptide when placed in solution results in a peptide being
“essentially the same as it was before the salt was formed,” i.e., “its structure
has not been markedly altered.” (Id. at 10; Ans. 7.)
Regarding the requirement in claim 9 that the peptide is acylated, the
Examiner further states:
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while it is appreciated that acylation of peptides has been
understood to alter the functional properties of the peptides, as
well as their structures, acylation is not necessarily evidence of
a transformation at the "hands-of-man", which distinguishes the
acylated peptide from its naturally occurring counterpart.
(Ans. 18.) The Examiner also finds that because prior art teaches that some
naturally occurring proteins have been found to be acylated and bound to
HLA class I in vivo, and that a large percentage “of all proteins [in humans]
receive an acetyl group at their N-terminus” that the claimed acylated
peptide consisting of the amino acid sequence of SEQ ID NO: 21 “is
certainly not distinguished from its natural counterpart,” though “[i]t is
however not known.” (Id. at 18–19.)
Regarding the requirement in claim 10 that the peptide is pegylated,
the Examiner further finds that the claim scope includes “non-covalent
pegylation” and such pegylation “does not alter the structure of the peptide,
at least not such that the reversal of the process cannot restore the peptide as
it originally occurred; and moreover, once such a peptide is released from
PEG, its biologic properties are unchanged.” (Id. at 20.) In addition, the
Examiner finds that, even as to covalent attachment, although such a
structure “is not naturally occurring” (id. at 21), “the difference is merely the
result of routine and conventional modification of the naturally occurring
peptide of the same amino acid sequence,” which “is not regarded as being a
‘marked’ difference” (id. at 20). “[T]he difference is not such that the
claimed invention has been transformed into a new and useful product
having a function that is significantly different from that of the naturally
occurring peptide of the same amino acid sequence.” (Id. at 21.)
Appellant argues that “the proper analysis for step 2A [in considering
patent-eligibility] is to look at what is claimed and determine whether it has
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an identical natural counterpart. If an identical counterpart to what is
claimed does not exist, that is the end of the analysis.” (Appeal Br. 14
(emphasis omitted).) Appellant points out that “there is no naturally
occurring peptide of SEQ ID No: 21 either in free form or in the form of a
pharmaceutically acceptable salt” and, therefore, “it is impossible for the
claims to be ‘directed’ to a judicial exception.” (Id. at 15.)
Appellant argues that it is an improper analysis under § 101 to
“parse[] [the claim] into i) the 9-amino acid and ii) a salt.” (Id. at 17.)
Appellant explains that
[a]n amino acid sequence having SEQ ID NO: 21 is either
found within a hydrophobic internal domain of a 1211 amino
acid NRCAM protein, or a peptide having SEQ ID NO: 21 is
found associated with an MHC-1 molecule on the surface of
antigen presenting cells.
(Id. at 17–18.) Undergirding Appellant’s argument is the testimony of
Dr. Lawrence Stern. (Id. at 20–24 (citing Stern Declaration3).)
Appellant further explains, with support from the testimony of
Dr. Stern, that the claimed peptide salt is markedly different from how the
peptide having the amino acid sequence of SEQ ID NO: 21 is found in
nature, i.e., “either within a twisted beta-strand domain of the NRCAM
protein or associated with an MHC-I molecule.” (Id. at 25–29.) In addition,
Appellant explains, with support from the testimony of Dr. Stern, that even
assuming a free peptide of SEQ ID NO: 21 exists in nature, the claimed
pharmaceutically acceptable salt is structurally and functionally different
from such a free peptide. (Id. at 29–30.)

3 Declaration of Dr. Lawrence Stern, dated May 16, 2018 (“Stern
Declaration”).
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Appellant argues that the Examiner “offered no evidence rebutting
any of Dr. Stern’s factual statements” or the “literature-based factual
evidence” in support thereof, and instead maintained the rejection of
ineligibility only on an analogy to dressing a snowman. (Id. at 32–34, 36–
39.)
Regarding the claims to the acylated and pegylated peptide consisting
of the amino acid sequence of SEQ ID NO: 21, Appellant indicates that
there is no record evidence that such compounds exist in nature. (Id. at 42.)
Analysis
35 U.S.C. § 101 defines patent-eligible subject matter. An invention
is patent-eligible if it claims a “new and useful process, machine,
manufacture, or composition of matter.” 35 U.S.C. § 101. The Supreme
Court, however, has carved out exceptions to what would otherwise appear
to be within the literal scope of § 101, e.g., “[l]aws of nature [and] natural
phenomena” such as products of nature that are considered “building blocks
of human ingenuity.” Alice Corp. v. CLS Bank Int’l, 573 U.S. 208, 216
(2014) (citing Ass’n for Molecular Pathology v. Myriad, 569 U.S. 576
(2013) and Mayo Collaborative Servs. v. Prometheus Labs, Inc., 566 U.S.
66, 89 (2012)). “[T]he ‘manifestations of laws of nature’ are ‘part of the
storehouse of knowledge,’ ‘free to all men and reserved exclusively to
none.’” Manual of Patent Examiner Procedure (“MPEP”) § 2106.04 (b)
(quoting Funk Bros. Seed Co. v. Kalo Inoculant Co., 333 U.S. 127, 130
(1948)). “When a law of nature or natural phenomenon is claimed as a
physical product, the courts have often referred to the exception as a
‘product of nature.’” MPEP § 2106.04(b)(II).
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The Supreme Court has established a two-step framework for
“distinguishing patents that claim laws of nature, natural phenomena, and
abstract ideas from those that claim patent-eligible applications of those
concepts.” Alice, 573 U.S. at 216. “First, we determine whether the claims
at issue are directed to” a patent-ineligible concept. Id. If so, “we consider
the elements of each claim both individually and ‘as an ordered
combination’ to determine whether the additional elements ‘transform the
nature of the claim’ into a patent-eligible application.” Id. at 217 (quoting
Mayo, 566 U.S. at 78–79).
The United States Patent and Trademark Office (“PTO”) issued 2019
Revised Patent Subject Matter Eligibility Guidance (“Guidance”), indicating
how the PTO would analyze patent eligibility under the Supreme Court’s
two-step framework. 84 Fed. Reg. 50–57 (January 7, 2019).4
Under the Guidance, in determining what concept a claim is “directed
to,” we first look to whether the claim recites any judicial exceptions,
including laws of nature, natural phenomena, and/or abstract ideas.
(Guidance, 84 Fed. Reg. at 53–54.) (“Step 2A, Prong One”). If it does, then
we look to whether the claim recites additional elements that integrate the
recited judicial exception into a practical application. (Id. at 54–55 (citing
MPEP § 2106.05(a)–(c), (e)–(h)).) (“Step 2A, Prong Two”).

4 “All USPTO personnel are, as a matter of internal agency management,
expected to follow the guidance.” Id. at 51; see also USPTO, October 2019
Update: Subject Matter Eligibility 1 (the “October 2019 Update”) (available
at https://www.uspto.gov/sites/default/files/documents/peg_oct_2019_
update.pdf).
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Only if a claim (1) recites a judicial exception and (2) does not
integrate that exception into a practical application, i.e., it is found to be
“directed to” a judicial exception, do we then look to whether the claim
contains an “‘inventive concept’ sufficient to ‘transform’” the claimed
judicial exception into a patent-eligible application of the judicial exception.
Guidance, 84 Fed. Reg. at 56; see also Alice, 573 U.S. at 221 (quoting Mayo,
566 U.S. at 82).
Claims alleged to be patent-ineligible because they recite products of
nature are properly analyzed under the framework of the Guidance. See
Guidance, 84 Fed. Reg. at 54 n.20 (“This notice does not change the type of
claim limitations that are considered to recite a law of nature or natural
phenomenon. For more information about laws of nature and natural
phenomena, including products of nature, see MPEP 2106.04(b) and (c).”).
Applying the Guidance and binding legal precedent, we disagree with
the Examiner’s conclusion that the claims are directed to patent-ineligible
subject matter. We address independent claim 1 as the representative claim
for our analysis. There is no dispute that claim 1, which recites a peptide in
the form of a pharmaceutically acceptable salt, is a composition and, thus,
falls squarely within the “composition of matter” statutory category.
Consequently, we proceed to the next steps of the analysis.
STEP 2A, Prong One:
In Step 2A, Prong One of the Guidance, we evaluate whether claim 1
recites a judicial exception, i.e., whether it sets forth or describes a product
of nature in accordance with the guidance in MPEP 2106.04 (b) and (c).
Guidance, 84 Fed. Reg. at 54; October 2019 Update.
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a. Product of Nature Analysis
Claim 1 requires a peptide “consisting of the amino acid sequence
GLWHHQTEV (SEQ ID NO: 21)” where that peptide is a pharmaceutically
acceptable salt. The claim includes recitation of a peptide having an amino
acid sequence that is undisputedly found in nature as part of a protein having
a larger sequence. As Appellant’s Specification indicates, SEQ ID NO: 21
is a peptide having an amino acid sequence from the 1211 amino acid
NRCAM protein, a single-pass type I transmembrane protein interacting
with ankyrin, and which is overexpressed in glioblastoma multiforme tissue
as compared to normal brain tissue. (Subst. Spec. 27 (Table 1), 44.)
However, as Appellant points out, the claim does not recite a free peptide,
but rather a pharmaceutically acceptable salt of that peptide. Thus, the
amino acid sequence of the peptide salt cannot be anything other than SEQ
ID NO: 21, but that peptide having the sequence must be in ionic
combination with another ion to form a pharmaceutically acceptable salt.
The claimed salt is a structurally different chemical composition than a free
peptide, as even the Examiner acknowledges (Ans. 5 (that the peptide is a
salt “simply means one or more of the amino acid residues of which the
peptide is composed has been ionized[ ] and has formed an ionic bond with
whatever cation (e.g., Na+) or anion (e.g., C1-) might be present.”). (See
Stern Declaration ¶ 20 (“Salts are formed when a compound that is ionized
in solution forms a strong ionic interaction with an oppositely charged
counterion, leading to neutralization of the charges . . . .”), id. ¶¶ 23–24
(“[P]eptides of any length . . . will therefore have a one free amino group
(NH2,) referred to as the amino terminus or N-terminus and one free
carboxyl group (COOH) referred to as the carboxyl or C-terminus . . . .
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[T]here can also be ionizable groups in the side chains (‘R’) of the amino
acid residues within the peptide.”).)
Appellant’s expert explained, with reference to numerous articles, that
a peptide with the amino acid sequence of SEQ ID NO: 21 would not exist
in the body as a salt. (Stern Declaration ¶¶ 32–33, 35.) Dr. Stern explained
that peptide fragments, such as a peptide having the amino acid sequence
SEQ ID NO: 21, that arise when proteins are degraded, are themselves
degraded within a few seconds if not associated with other proteins involved
in degradation, ER transport and loading of the peptide onto MHC-1
molecules. (Stern Declaration ¶ 32.) Dr. Stern notes that “[i]n the absence
of peptide binding, neither the peptide nor the MHC molecule by itself is
stable, or persists” in nature. (Id. ¶ 33 (emphasis omitted).)
Dr. Stern further explains that even if the free peptide existed in the
cell, “there is no acid-base reaction that could occur in the cytoplasm or ER
of a cell . . . that would result in formation of a peptide salt.” (Id. ¶ 35.)
That is because “[t]he formation of salts requires specific combinations of
acids or bases in specific concentrations, at a defined ratio (stoichiometry),
so that there is a set number of moles of acid and moles of base in a
controlled environment[, and] [t]he cytoplasm of a cell is not such an
environment.” (Id.) Dr. Stern notes that the cytoplasm “would not contain
either the peptides or the acid or base counterpart in sufficient quantities in
sufficient proximity to each other to form a peptide salt.” (Id.) Furthermore,
Dr. Stern explains that “[e]ven if all the water in cell were removed, specific
salts would not form, because of the highly complex mixtures of anions and
cations present.” (Id.)
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The Examiner has not provided any evidence in contravention of the
foregoing testimony by Dr. Stern. Rather, the Examiner asserts that peptide
in salt form, nevertheless, will consist of the amino acid SEQ ID NO: 21 and
thus is not “significantly changed.” (Ans. 5, 7.) The Examiner also asserts,
without evidentiary support, that because of the presence of certain amino
acids in the sequence “it is conceivable that the salt of the peptide may have
formed by association with two cations and one anion.” (Ans. 6–7.) The
Examiner states:
naturally occurring peptides such as the peptide of SEQ ID
NO: 21 are expected to exist at physiological pH (pH = 7.4) in
the body of human in or on the surface of a cell expressing
NRCAM in the context of an HLA-A2 class I complex . . . .
Furthermore, as example, it is known that most of the Na+ in
the body is present in the blood (plasma) and the interstitial,
extracellular fluid, which surrounds the cells[ ], where it might
freely associate with the negatively charged carboxyl terminus
and/or the negatively charged glutamic acid residue of the
peptide lying the in the cleft of the HLA complex to form a salt
thereof.
(Ans. 10.)
Also, relying on general principles of chemistry, the Examiner posits
that because the peptide is present in an aqueous solution in vivo within the
cytosol, the endoplasmic reticulum, and at the surface of cells in complex
with an HLA class I molecule, it will be ionized and because there are
“counterions of the appropriate charge” naturally present in each situation in
the body, a salt will form. (Ans. 11–15.)
The Examiner’s assertion that, in general, the peptide fragment of
protein degraded by a proteasome will naturally form a salt in the cytosol,
the ER, or the MHC because there are counterions such as sodium, chloride
and potassium around in the cell lacks any evidentiary foundation. And, it is
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contradicted by the testimony of Dr. Stern that salt formation requires
specific combinations of acids or bases in specific concentrations, at a
defined ratio (stoichiometry), so that there is a set number of moles of acid
and moles of base in a controlled environment. The Examiner did not
establish that the cytosol, the ER and the MHC in vivo are such a controlled
environment with respect to peptide fragments of the protein degraded by a
proteasome.
In addition, the Examiner’s position that the free peptide is extant in
the first place for long enough to form a salt is contradicted by Dr. Stern’s
testimony that any free peptide of the collagen protein degraded by a
proteasome would be rapidly degraded if it is not associated with certain
other proteins in the cytosol or in transport to the endoplasmic reticulum or
when bound in the MHC.
While an amino acid sequence consisting of SEQ ID NO: 21 is
unquestionably identical to the peptide sequence found in NRCAM, which
Appellant does not dispute, we conclude that the preponderance of the
evidence favors finding that the claimed pharmaceutically acceptable salt of
the peptide consisting of the amino acid sequence of SEQ ID NO: 21 is not a
product that occurs in nature.
Furthermore, we disagree with the Examiner’s conclusion that the
claimed invention is not markedly different from a naturally occurring
peptide consisting of an amino acid sequence of SEQ ID NO: 21.5 The

5 We note, but do not find it necessary to respond to, Appellant’s arguments
concerning any alleged misapplication of law in the MPEP. (Appeal Br. 10.)
We need not address this argument because we conclude that the Examiner
erred in evaluating the claimed invention as a whole.
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Examiner’s analysis does not properly address the claimed structure, as
discussed above. The markedly different characteristics analysis is not
applied to the component parts of the claimed salt, but to the compound as a
whole. See, e.g., MPEP § 2106.04(c)(I)(A).
As the MPEP notes,
The courts have emphasized that to show a marked difference, a
characteristic must be changed as compared to nature, and
cannot be an inherent or innate characteristic of the naturally
occurring counterpart or an incidental change in a characteristic
of the naturally occurring counterpart. Myriad, 569 U.S. at 580
[ ]. Thus, in order to be markedly different, applicant must
have caused the claimed product to possess at least one
characteristic that is different from that of the counterpart.
Id. § 2106.04(c)(II)(C). As the MPEP further explains, the “[m]arkedly
different characteristics can be expressed as the product’s structure, function,
and/or other properties, and are evaluated based on what is recited in the
claim on a case-by-case basis.” Id. § 2106.04(c)(II).
The question for consideration here is whether the structure claimed is
different from the peptide sequence as it is found in nature. As just
discussed, the evidence of record favors Appellant’s position that the
claimed peptide does not exist in nature as a free peptide.
Furthermore, it cannot be said that the pharmaceutically acceptable
salt of amino acid peptide of SEQ ID NO: 21 is merely an isolated
component of a larger structure known to be present in nature, similar to
DNA isolated from the human genome. Cf. Myriad, 569 U.S. at 593 (“Nor
are Myriad’s claims saved by the fact that isolating DNA from the human
genome severs chemical bonds and thereby creates a nonnaturally occurring
molecule.”); see also Roche Molecular Sys., Inc. v. CEPHEID, 905 F.3d
1363 (Fed. Cir. 2018) (finding similar to the claimed DNA at issue in
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Myriad, that the claimed primers were necessarily present in the natural
genome of Mtb). In Myriad, the Supreme Court determined that naturally
occurring, but isolated, DNA fell within the product of nature exception
because “Myriad’s claims . . . do [not] rely in any way on the chemical
changes that result from the isolation of a particular section of DNA.”
Myriad, 569 U.S. at 593. The Court in Myriad, however, also noted that
“creation of a cDNA sequence from mRNA results in an exons-only
molecule that is not naturally occurring” and determined that such a
chemical construct is patent-eligible. Id. at 594. Here, the markedly
different characteristic for the claimed peptide is not merely due to the
breaking of chemical bonds of the protein, but it is rather based on chemical
differences between the NRCAM protein as it is found in nature, and the
claimed pharmaceutically acceptable salt of the peptide of SEQ ID NO: 21
that is in ionic interaction with an oppositely charged counterion. That
structural difference is not an inherent or innate characteristic of the
naturally occurring peptide as it is found in nature or an incidental change as
Appellant’s expert testimony and underlying supporting evidence
establishes.
We conclude that, like the cDNA in Myriad, the pharmaceutically
acceptable salt of the peptide consisting of amino acid SEQ ID NO: 21 is
markedly different from the naturally occurring peptide sequence of amino
acid SEQ ID NO: 21 found in NRCAM.6

6 In addition to this structural difference, Dr. Stern contends that the free
peptide would be poorly soluble in aqueous solution (Stern Declaration ¶ 39)
whereas “[s]alts of hydrophobic peptides have been shown improve their
solubility in aqueous solutions, just as salts of other compounds improve
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Accordingly, under Guidance Step 2A, Prong 1, we conclude that the
composition of claim 1 does not recite a product of nature, and thus is not
directed to a patent ineligible judicial exception. Our analysis of the issue
need not proceed further.
We similarly conclude that claims 9, 10, 13, and 14, which recite an
“acylated” or a “pegylated” “peptide consisting of the amino acid sequence
of GLWHHQTEV (SEQ ID NO: 21) or a pharmaceutically acceptable salt
thereof” are not directed to a product of nature. The Examiner does not
dispute that these claims are directed to a structure that is chemically
different than that found in nature. (Ans. 18 (“[I]t is appreciated that
acylation of peptides has been understood to alter the functional properties
of the peptides, as well as their structures”); Ans. 19–20 (covalent
attachment of PEG “is expected to alter, not only the structure of the peptide,
but also its functional characteristics” and non-covalent pegylation is a
structural alteration that can be reversed to “restore the peptide as it
originally occurred”). The Examiner contends that even with the structural
differences, the peptide sequence itself is not changed by the modifications.
(Id. at 19–23.)

their solubility” (id. ¶ 41). He also contends that “[p]eptides are not very
stable in free form, without modifications” (id. ¶ 42) and that “the peptide
claimed in the Immatics application can undergo hydrolysis in aqueous
solution in free form” (id. ¶ 43), whereas “[f]ormation of peptide salts
stabilizes the peptides from physical degradation, discussed above, to some
extent” (id. ¶ 46). In light of our conclusion regarding the marked structural
difference, we need not address Appellant’s additional argument and
testimony of Dr. Stern that the physical properties of the pharmaceutically
acceptable salt of the claimed peptide fragment is markedly different than a
free peptide fragment if it existed in nature.
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The Examiner’s evidence offered in the Answer that an acylated
peptide degradation product has been found bound to an HLA class I
molecule does not establish the claimed acylated peptide having the
specifically claimed sequence occurs naturally in the human body, or that
this is the case for any peptide derived endogenously from the breakdown of
a protein by a proteasome, nor does it contradict Appellant’s expert’s
testimony and underlying evidence relied upon that such does not exist. (See
Stern Declaration ¶ 69.)
Furthermore, the Examiner’s position that even with the structural
differences because of the addition of an acyl group or PEG, the peptide
sequence itself is not changed by the modification is an improper analysis.
As explained, the markedly different characteristics analysis is not applied to
the component parts of the claimed acylated or pegylated peptide claimed,
but to the compound as a whole. The difference in structure is more than
mere excising a DNA or a peptide from a larger protein; the structure of
these compounds as a whole, just as with the pharmaceutically acceptable
salt of claim 1, chemically speaking, is different from that which is naturally
occurring. That is so even if the structure can be arrived at using routine and
conventional chemical modifications. An analysis of whether the activity to
arrive at that different structure may not be an inventive concept is not a
relevant consideration here. MPEP § 2106.04(c) (“[O]nce a markedly
different characteristic in [a] product is shown, no further analysis would be
necessary for eligibility because no product of nature exception is recited
(i.e., Step 2B is not necessary because the answer to Step 2A is NO).”).
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In light of the foregoing, we do not affirm the Examiner’s rejection of
claims 1, 3, 4, 9–14, and 21–26 under 35 U.S.C. § 101 as being directed to
patent-ineligible subject matter.
II. Non-statutory double patenting
Appellant did not argue the substance of this rejection nor has it
indicated that a terminal disclaimer was filed. Thus, we summarily affirm
the Examiner’s rejection based on the judicially created doctrine of
obviousness-type double patenting for the reasons advanced by the
Examiner in the Final Rejection. See MPEP § 1205.02 (“If a ground of
rejection stated by the examiner is not addressed in the appellant’s brief,
appellant has waived any challenge to that ground of rejection and the Board
may summarily sustain it, unless the examiner subsequently withdrew the
rejection in the examiner’s answer.”).
DECISION SUMMARY
In summary:
Claims
Rejected
35 U.S.C. § Reference(s)/Basis Affirmed Reversed
1, 3, 4, 9–
14, 21–26
101 Eligibility

1, 3, 4, 9–
14, 21–26
1, 3, 4, 9–
14, 21–27
Nonstatutory Double
Patenting
1, 3, 4, 9–
14, 21–27

Overall
Outcome
1, 3, 4, 9–
14, 21–27

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). See 37 C.F.R.
§ 1.136(a)(1)(iv).
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AFFIRMED