Ex Parte Gellman et al

Patent Trials and Appeals Board

Apr 17, 2019

14312012 - (D) (P.T.A.B. Apr. 17, 2019)

UNITED STA TES p A TENT AND TRADEMARK OFFICE
APPLICATION NO. FILING DATE
14/312,012 06/23/2014
60961 7590 04/19/2019
Intellectual Property Dept/De Witt LLP
Wisconsin Alumni Research Foundation
2 East Mifflin Street,
Suite #600
Madison, WI 53703-2865
FIRST NAMED INVENTOR
Samuel H. Gellman
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
ATTORNEY DOCKET NO. CONFIRMATION NO.
09820579-Pl30312US03 3681
EXAMINER
MIKNIS, ZACHARY J
ART UNIT PAPER NUMBER
1654
NOTIFICATION DATE DELIVERY MODE
04/19/2019 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):
IP-DOCKET@dewittllp.com
PTOL-90A (Rev. 04/07)
UNITED STATES PATENT AND TRADEMARK OFFICE
BEFORE THE PATENT TRIAL AND APPEAL BOARD
Ex parte SAMUEL H. GELLMAN,
ROSS W. CHELOHA, and THOMAS J. GARDELLA
(APPLICANTS: Wisconsin Alumni Research Foundation and
The General Hospital Corporation d/b/a Massachusetts General Hospital)
Appeal2018-007374
Application 14/312,012 1
Technology Center 1600
Before DONALD E. ADAMS, TA WEN CHANG, and
JOHN E. SCHNEIDER, Administrative Patent Judges.
ADAMS, Administrative Patent Judge.
DECISION ON APPEAL
This Appeal under 35 U.S.C. § 134(a) involves claims 1, 10-18, 20,
and 21 (App. Br. 2). Examiner entered a rejection under 35 U.S.C. § 103(a).
We have jurisdiction under 35 U.S.C. § 6(b ).
We REVERSE.
1 Appellants identify "Wisconsin Alumni Research Foundation" as the real
party in interest (Appellants' December 20, 2017 (App. Br.) 2).
Appeal2018-007374
Application 14/312,012
STATEMENT OF THE CASE
Appellants' independent claims 1 and 20 are representative and
reproduced below:
1. An isolated, unnatural peptide analog comprising:
PTH, a parathyroid hormone receptor (PTHR-1, PTHR-
2) agonist- or inverse agonist effective fragment of PTH, a
parathyroid hormone related protein (PTHrP), a PTHR-1 or
PTHR-2 agonist-, or inverse agonist-effective fragment of
PTHrP, M-PTH, a PTHR-1 or PTHR-2 agonist-, or inverse
agonist-effective fragment ofM-PTH, BA058, or a PTHR-1 or
PTHR-2 agonist-, or inverse agonist-effective fragment of
BA058, in which at least five non-adjacent a-amino acid
residues are replaced with /J-amino acid residues; and
salts thereof.
(App. Br. Claims Appendix 1 (emphasis added).)
20. A pharmaceutical composition for treating
hypoparathyroidism, the composition comprising a parathyroid
hormone receptor agonist effective amount of PTH, a
parathyroid hormone receptor (PTHR-1, PTHR-2) agonist-
effective fragment of PTH, a parathyroid hormone related
protein (PTHrP), a PTHR-1 or PTHR-2 agonist effective
fragment of PTHrP, M-PTH, a PTHR-1 or PTHR-2 agonist-
effective fragment ofMPTH, BA058, or a PTHR-1 or PTHR-2
agonist-effective fragment ofBA058, in which at least five
non-adjacent a-amino acid residues are replaced with /J-amino
acid residues, in combination with a pharmaceutically suitable
earner.
(Id. at 1-2 (emphasis added).)
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Appeal2018-007374
Application 14/312,012
Grounds of rejection before this Panel for review:
Claims 1, 10-18, and 20 stand rejected under 35 U.S.C. § I03(a) as
unpatentable over the combination of Home2 and Chorev. 3
ISSUE
Does the preponderance of evidence relied upon by Examiner support
a conclusion of obviousness?
FACTUAL FINDINGS (FF)
FF 1. Home "is directed to a method of making polypeptide compounds
comprising alpha- and beta-amino acid residues, the compounds produced
thereby, and use of the compounds as pharmaceutically active agents to treat
diseases in animals, including humans" (Home ,r 3; see generally Ans. 4 4).
FF 2. Home discloses, inter alia,
A method of fabricating biologically active, unnatural
polypeptides, the method comprising:
(a) selecting a biologically active polypeptide or biologically
active fragment thereof having an amino acid sequence
comprising a-amino acid residues; and
(b) fabricating a synthetic polypeptide that has an amino acid
sequence that corresponds to the sequence of the
biologically active polypeptide or fragment of step (a),
wherein
(i) in the synthetic polypeptide between about 14% and
about 50% of the a-amino acid residues found in the
biologically active polypeptide or fragment of step (a)
are replaced with B-amino acid residues;
2 Home et al., US 2010/0099185 Al, published Apr. 22, 2010.
3 Chorev et al., US 2006/0058230 Al, published Mar. 16, 2006.
4 Examiner's May 4, 2018 Answer.
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Appeal2018-007374
Application 14/312,012
(ii) in the synthetic polypeptide the B-amino acid residues
and the a-amino acid residues are distributed in a
repeating pattern; and
(iii) the synthetic polypeptide has a length of from about 10
residues to about 100 residues and comprises at least
two B-amino acid residues.
(Home 34: Claim 1; see also id. at 35: Claims 2, 3, 6, and 7; see also Ans.
4.)
FF 3. Home discloses that "[t]he method of fabricating biologically active,
unnatural polypeptides according to any one of claims 1 to 7, wherein the
repeating pattern of B-amino acid residues and a-amino acid residues is
selected from the group consisting of ( aaaaaaB), ( aaaaaB), ( aaaaB),
(aaaB), (aaB), (aaBaaaB), (aaBaBaB), and (aB)" (Home 35: Claim 9).
FF 4. Home discloses that its "method can also be used to "fabricate a/B-
polypeptides, on a rational basis, to treat disorders relating to bone and
calcium metabolism by targeting the interactions between parathyroid
hormone and its receptors (PTHlR and PTH2R)" (Home ,r 97; see Ans. 4--
5).
FF 5. Home's disclosure
includes compounds ... for use as pharmaceuticals and the use
of the compounds for the manufacture of a medicament for the
treatment of any disease associated with any of the assays
described [therein and] ... the use of a compound fabricated
according to [Home's] claimed method as a pharmaceutical,
and pharmaceutical compositions comprising an effective
amount of such a compound together with a pharmaceutically
acceptable diluent or carrier.
(Home ,r 108; see Ans. 5.)
FF 6. Examiner finds that Home fails to disclose PTH, a parathyroid
hormone receptor (PTHR-1, PTHR-2) agonist- or inverse agonist effective
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Appeal2018-007374
Application 14/312,012
fragment of PTH, a parathyroid hormone related protein (PTHrP), a PTHR-1
or PTHR-2 agonist-, or inverse agonist-effective fragment of PTHrP, M-
PTH, a PTHR-1 or PTHR-2 agonist-, or inverse agonist-effective fragment
ofM-PTH, BA058, or a PTHR-1 or PTHR-2 agonist-, or inverse agonist-
effective fragment of BA058 (see Ans. 5 (Home fails to "teach any of the
base peptides as found in [Appellants'] claim 1"); cf App. Br. Claims
Appendix 1).
FF 7. Chorev discloses "novel parathyroid hormone [PTH] analogs and
parathyroid hormones-related protein [PTHrP] analogs [and] ... methods of
using these analogs to treat osteoporosis, promote the formation of bone, and
inhibit bone loss" (Chorev, Abstract; see id. ,r 19; Ans. 5).
FF 8. Chorev discloses "analogs of PTH or PTHrP that include one or
more amino acid substitutions at positions 16, 17, 18, 19 and/or 20," wherein
Chorev prefers that these specific "amino acid substitutions are B3-residues
(B-substituted B-amino acid residues) although B2-residue substitutions ( a-
substituted B-amino acid residues) also are provided" (Chorev ,r 20; see
generally Chorev ,r 15; see also Ans. 5).
FF 9. Chorev further discloses a-amino acid substitutions at additional
amino acid positions (Chorev ,r,r 30-39).
FF 10. Peggion discloses structure-function studies of PTH 1-34 analogous
containing B-amino acid residues in positions 11-13 (see Peggion, Title; see
also id. 8165: Table 1; Ans. 9-11, 13, and 16).
ANALYSIS
Based on the combination of Home and Chorev, Examiner concludes
that, at the time Appellants' invention was made, it would have been prima
facie obvious to use Chorev's PTH or PTHrP proteins in Home's method of
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Appeal2018-007374
Application 14/312,012
making polypeptide compounds comprising alpha- and beta-amino acid
residues and, thereby, "arrive at [Appellants'] claimed peptide analogs of
PTH or PTHrP" (Ans. 5). In addition, Examiner finds that the preamble of
Appellants' claim 20 states the intended use of the claimed pharmaceutical
composition, which "does not impart any structure that is not found in the
body of [Appellants'] claim [20], and[,] as such[,] is not considered ... a
limitation" (id. at 6-7). Therefore, Examiner concludes that the combination
of Home and Chorev makes obvious a pharmaceutical composition within
the scope of Appellants claim 20 (id. at 7). Although Examiner did not
include Peggi on in the statement of the rejection, we acknowledge
Examiner's reference to Peggion in support of Examiner's assertion that
B-amino acid substitutions outside of the amino acid positions disclosed by
Chorev would have been prima facie obvious to a person of ordinary skill in
this art (see generally Ans. 9). We are not persuaded.
As Appellants explain, although Home discloses "peptides having a
repeating pattern of a and B residues," Home "in no way applies that pattern
to PTH" or PTHrP (App. Br. 4). Although Chorev discloses analogs of PTH
and PTHrP peptides, "Chorev explicitly and exclusively teaches that there
are only five adjacent positions within PTH that can be modified, namely
residues 16, 17, 18, 19, and 20" (id.). "Thus, [ Appellants explain,] when
Home ... is combined with Chorev ... , only the five residues as taught by
Chorev ... (positions 16-20) are taught as being suitable residues for
modification" with a B-amino acid (id.; see also id. at 5 ("Modifying Home
... using the teachings of Chorev does not yield a PTH analog having five
'non-adjacent' B-amino acid residues as required by both [of Appellants'
independent claims,] Claim 1 and Claim 20")). In addition, Appellants
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Application 14/312,012
explain that, notwithstanding Examiner's assertion to the contrary, although
Chorev discloses "a host of other amino acid substitutions that alter one a-
amino acid for a different a-amino acid residue ... Chorev explicitly teaches
that only residues 16, 17, 18, 19, and 20 may be mutated to contain a beta-
amino acid residue" (id.). We agree with Appellants (see FF 1-9).
Appellants further explain that Examiner's "reliance on Peggion is
improper because most of Peggion's substitutions insert a different alpha-
amino acid residue, rather than a beta-amino acid residue," specifically
"Peggion only inserted beta-alanine residues at positions 11, 12, or 13, or a
beta-homo leucine residue at position 11 ... [and] never made or mentioned
any peptide having a beta-amino acid substitution[] at non-adjacent
positions" (Reply Br. 2). We agree with Appellants (see FF 10).
Taken together, the combination of Home, Chorev, and Peggion
suggests that B-amino acids may be substituted into PTH at positions 11-13
or 16-20, not "that residues 11-20 of PTH are areas ripe for B-amino acid
substitutions" (Reply Br. 2). To emphasize this point, Appellants explain
that although Chorev discloses a number of different PTH amino acid
modifications, the only modifications that involve a B-amino acid are amino
acid residues 16-20 (see Reply Br. 3--4). Similarly, although Peggion
discloses a number of PTH amino acid modification, the only modifications
that involve a B-amino acid are amino acid residues 11-13 (see FF 9; see
generally Reply Br. 2). Thus, taken together the prior art relied upon by
Examiner suggests that there are two sets of amino acid residues that may be
modified with a B-amino acid, i.e. residues 11-13 and 16-20. Examiner
failed, however, to establish an evidentiary basis on this record to support a
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Application 14/312,012
conclusion that that any amino acids within these two sets may be combined
to arrive at Appellants' claimed invention.
In sum, we agree with Appellants and find that Examiner failed to
establish an evidentiary basis on this record to support a conclusion that the
combination of Home and Chorev, with or without Peggion, makes obvious
Appellants' claimed invention which requires, inter alia, that at least five
non-adjacent a-amino acid residues from a peptide selected from the group
consisting of:
PTH, a parathyroid hormone receptor (PTHR-1, PTHR-2)
agonist- or inverse agonist effective fragment of PTH, a
parathyroid hormone related protein (PTHrP), a PTHR-1 or
PTHR-2 agonist-, or inverse agonist-effective fragment of
PTHrP, M-PTH, a PTHR-1 or PTHR-2 agonist-, or inverse
agonist-effective fragment ofM-PTH, BA058, or a PTHR-1 or
PTHR-2 agonist-, and inverse agonist-effective fragment of
BA058; and salts thereof,
are replaced with B-amino acid resides.
CONCLUSION
The preponderance of evidence relied upon by Examiner does not
support a conclusion of obviousness. The rejection of claims 1, 10-18, and
20 under 35 U.S.C. § 103(a) as unpatentable over the combination of Home
and Chorev is reversed.
REVERSED
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