13122758 (P.T.A.B. Dec. 12, 2018)

Ex Parte Takamura et al

Patent Trial and Appeal BoardDec 12, 2018

13122758 (P.T.A.B. Dec. 12, 2018)

UNITED STA TES p A TENT AND TRADEMARK OFFICE APPLICATION NO. FILING DATE 13/122,758 04/06/2011 24280 7590 12/14/2018 CHOATE, HALL & STEWARTLLP TWO INTERNATIONAL PLACE BOSTON, MA 02110 FIRST NAMED INVENTOR Kentaro Takamura 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. 2004837-0057 2460 EXAMINER ORWIG, KEVIN S ART UNIT PAPER NUMBER 1611 NOTIFICATION DATE DELIVERY MODE 12/14/2018 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): patentdocket@choate.com jnease@choate.com PTOL-90A (Rev. 04/07) UNITED STATES PATENT AND TRADEMARK OFFICE BEFORE THE PATENT TRIAL AND APPEAL BOARD Ex parte KENT ARO T AKAMURA, SATOSHI GOJO, and SATORU KOBAYASHI Appeal2017-004462 Application 13/122,758 Technology Center 1600 Before JEFFREY N. FRED MAN, MICHAEL J. FITZPATRICK, and RACHEL H. TOWNSEND, Administrative Patent Judges. FREDMAN, Administrative Patent Judge. DECISION ON APPEAL This is an appeal 1,2,3 under 35 U.S.C. Â§ 134 involving claims to a peptide for hemostasis. The Examiner rejected the claims as obvious. We have jurisdiction under 35 U.S.C. Â§ 6(b ). We reverse. 1 Appellants identify the Real Party in Interest as 3-D MATRIX, LTD (see App. Br. 3). 2 We have considered and herein refer to the Specification of Apr. 6, 2011 ("Spec."); Final Office Action of Mar. 1, 2016 ("Final Action"); Appeal Brief of Nov. 1, 2016 ("App. Br."); Examiner's Answer of Nov. 28, 2017 ("Ans."); and Reply Brief of Jan. 27, 2017 ("Reply Br."). 3 An oral hearing was held December 6, 2018. Appeal2017-004462 Application 13/122,758 Statement of the Case Background "Tissue occlusion to prevent leakage of body fluids (blood, tissue fluids and the like) caused by tissue damage have major significance in clinical situations, including surgery" (Spec. ,r 2). "Hemostasis is considered clinically important for the following reasons. 1. Blood loss is a major cause of death ... 2. Hemorrhage during surgery is a major concern ... 3. Hemorrhage is also a problem with minimally invasive surgery" (Spec. "Self-assembling peptides have a property whereby the peptide molecules form regularly arranged self-assemblies according to their amino acid sequence" (Spec. ,r 13). The self-assembly results in aggregates of nanofibers that exhibit a gel-like form. (Spec. ,r,r 16-17). "Since the peptide hydrogel is biodegradable and its decomposition product does not adversely affect tissue, while it is also highly bioabsorbable, it is suitable for cellular engraftment and growth" (Spec. ,r 19). "The application of self-assembling peptides for hemostasis is indicated in Patent document 1 [, International Patent Publication No. W02006-116524], but the video showing hemostasis at a hepatic incision site, provided in an article cited in the examples thereof, shows persistent blood leakage from the end of the incision site, and the reported complete hemostasis was not achieved" (Spec. ,r 21 ). "The objective of the present invention is to provide a self-assembling peptide tissue occluding agent that can effectively occlude sites of tissue damage in large mammals including humans and that does not carry the risk 2 Appeal2017-004462 Application 13/122,758 of infection by viruses and the like, as well as a method for use of the same." (Spec. ,r 22). The Claims Claim 16 is on appeal and reads as follows: 16. A liquid composition comprising a peptide that consists of SEQ ID N0:2, 4 the composition being characterized by an ability to occlude sites of tissue damage in mammals, wherein the liquid composition gels by self-assembly into a ~-sheet structure at physiological pH in the presence of monovalent alkali metal ions. The Rejection5 The Examiner rejected claim 16 under 35 U.S.C. Â§ I03(a) as obvious over Horii6 and 3D Matrix7 (Final Act. 4--8). The Examiner finds "Horii discloses self-assembling peptides" that comprise "a self-assembling domain, made up of peptides that self-assemble into ~-sheets ... in the presence of cations" (Final Act. 4). The Examiner finds "Horii teaches and exemplifies acetylation at the N terminus of the peptides" because "neutralization of charges at the N- and C- termini may facilitate self-assembly" (id. at 5). The Examiner finds "Horii teaches amphiphilic peptides containing the IEIK repeat in at least any length from 4 We note that SEQ ID NO: 2 is, in the single letter code used to represent amino acids, IEIKIEIKIEIKI or (IEIK)3I (see Sequence Listing filed Apr. 6, 2011). 5 The Examiner withdrew the rejection under 35 U.S.C. Â§ 112, second paragraph and identified the obvious-type double patenting rejection as moot (see Ans. 2). 6 Horii et al., US 2009/0162437 Al, published June 25, 2009. 7 3D Matrix, WO 2006/014570 A2, published Feb. 9, 2006. 3 Appeal2017-004462 Application 13/122,758 (IEIK)2 (8mer) to (IEIK)4 (16mer) including all lengths (e.g. 13 amino acids) encompassed within this range" (id. at 6). The Examiner acknowledges that "[ w ]hile Horii teaches self- assembling sequences encompassing that instantly claimed (i.e. SEQ ID NO: 2), Horii's peptides comprise two domains" (Final Act. 6). The Examiner finds 3D Matrix teaches "peptide compositions wherein the peptides have alternating hydrophilic and hydrophobic amino acids and self assemble into ~-sheet structures in the presence of monovalent cations" (Final Act. 6-7). The Examiner finds 3D matrix teaches "peptides comprising the IEIK repeat motif' and "solutions of the peptides that form gels" that "may be used to facilitate wound healing, for example in hemostasis" (id. at 7). The Examiner determines that it would have been obvious to use solutions of the self-assembling, ~-sheet-forming peptide domains disclosed by Horii on their own. One would be motivated to do so to provide a means for occluding sites of body fluid leakage, e.g. to stop blood flow around blood vessels that have been damaged during surgery. One would have had a high expectation of success since [3D Matrix] teaches substantially similar amphiphilic ~-sheet peptides for this same application and in fact teaches an overlapping set of self- assembling, ~-sheet-forming peptides as those taught by Horii. (Final Act. 7). The issues with respect to this rejection are: (i) Does the evidence of record support the Examiner's conclusion that Horii and 3D Matrix render claim 16 primafacie obvious? 4 Appeal2017-004462 Application 13/122,758 (ii) If so, have Appellants presented evidence of secondary considerations, that when weighed with the evidence of obviousness, is sufficient to support a conclusion of non-obviousness? Findings of Fact 1. Horii teaches "to modify self-assembling peptides by incorporating an additional domain that does not self-assemble, while still permitting assembly of the self-assembling portion. The additional domain can confer a variety of properties on the resulting peptide" (Horii ,r 10). 2. Horii teaches "[m]aterials formed by self-assembly of the peptides have a wide variety of uses, particularly in the areas of cell culture, tissue engineering, and tissue repair" (Horii ,r 10). 3. Horii teaches "the peptide solution before gellation can be a non-viscous fluid, viscous fluid or Sol form. Exemplary gellation agents include, but are not limited to, electrolytes (e.g., NaOH, KCl, NaCl, saline (NaCl-aqueous)" (Horii ,r 124). 4. Horii teaches "[p ]referred peptides assume regular secondary structures, such as ~-sheet structures, in solution ( e.g., aqueous solution)" (Horii ,r 196). 5. Horii teaches "the self-assembling portion of a self-assembling peptide is about 8-24, frequently about 12-20 ... amino acids" (Horii ,r 136). 6. Horii teaches exemplary self-assembling peptides in Table 21, reproduced in part below: 5 Appeal2017-004462 Application 13/122,758 TABLE 21 Fun,;t.ional peDt~des b.~sed on various s~lf~assembli~19 se,~u.ence SEQ ID NO+ l3 l},c-IEIKIEIKIG(lPRGSÂ¥RGDS-COllH .. 1 Eepetitive RGD binding oieq:,..i.en,;::e Â£ EQ El 1:JO" H Ac:- I EI KI EI KIGGPFSÂ£1'KT- Câ€¢:J.l:JH:, "Functionalized peptides based on (IEIK)2 ... were synthesized as shown in Table 21" (Horii ,r 464). 7. Horii teaches "(IEIK)2 is short sequence consists from 8 residues, but forms stiffer gels compared to (RADA)4 as it uses Isoleucine (I) as hydrophilic amino acid components which are less flexible to Alanine (A). Stiffer gels can be obtained by making the self-assembling repetitive sequence longer, such as (IEIK)3, (IEIK)4" (Horii ,r 462). 8. 3D Matrix teaches "improved materials of biological origin that have improved compatibility, present a reduced risk of contamination, and provide the proper biomechanical characteristics for tissue repair are desirable" (3D Matrix 2:3-5). 9. 3D Matrix teaches "a composition including amphiphilic peptide chains having alternating hydrophilic and hydrophobic amino acids that are complementary and structurally compatible and self-assemble into a beta-sheet macroscopic scaffold. The peptide chains contain at least 8 amino acids" (3D Matrix 5:13-16). 10. 3D Matrix teaches "an aqueous solution comprising the peptide chains. The solution may form a hydrogel that is stable with respect to mechanical agitation" (3D Matrix 5: 19-21 ). 6 Appeal2017-004462 Application 13/122,758 11. 3D Matrix teaches the peptide solutions may be formed into a stable scaffold by exposure to a monovalent salt solution. Sufficient electrolyte is added to the solution to initiate self-assembly of the peptides into a beta-sheet macroscopic structure ... Suitable electrolytes include, but are not limited to, Li+, Na+, K+, and cs+. (3D Matrix 21:20-27). 12. Table 1 of 3D Matrix is reproduced in part below: Â·'}"ah}/;;, 1Â·Â· Ren"l"'Qit:!enro+iy? Qli111c- A 0 ~Â·emt.linu I1eÂ· nf;,,l.'!>