DETAILED ACTION
Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Continued Examination Under 37 CFR 1.114
A request for continued examination under 37 CFR 1.114, including the fee set forth in 37 CFR 1.17(e), was filed in this application after final rejection. Since this application is eligible for continued examination under 37 CFR 1.114, and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114. Applicant's submission filed on 4/23/2025 has been entered.
Claim Status
Claims 9-12 and 39-42 are pending.
Claims 1-8, 13-38, and 43-61 are cancelled.
Claims 9-12 and 39-42 have been examined.
Priority
This application is a 371 of PCT/US2017/043614 07/25/2017
PCT/US2017/043614 has PRO of 62366370 07/25/2016
Information Disclosure Statement
The information disclosure statement (IDS) submitted on 4/23/2025 is in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement has been considered by the examiner.
Withdrawn Rejection
The rejection of claims 9-13, 24, 39-43, and 54 under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, is withdrawn because the argument of a person in the art would have known a buffer with an osmolarity value greater than 290 mOsm and a pH of between 6.5 and 8.5 is persuasive (Remarks, p7, last para to p8, para 1).
All prior art rejections are withdrawn because the amendments overcome the rejections of record.
New Ground of Rejection
Claim Rejections - 35 USC § 103
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
Claims 9-12 and 39-42 are rejected under 35 U.S.C. 103 as being unpatentable over Wu et al. (Cryst. Growth Des. 2015, 15, 2452−2460, previously cited 7/29/2022) in view of Bohner et al. (Biomatter, 2013; 3:2, e25103), Benedict et al., (US 2007/0141103 A1, previously cited 7/29/2022), Barbosa-Canovas (book, 1996, ISBN 978-1-4419-4723-9), Natan et al. (PLoS ONE. 2009; 4(4): e5240), Behnam (US 2007/0098756 A1, previously cited 7/29/2022), Will et al. (J Assist Reprod Genet (2011) 28:711–724) and Qian et al. (J Biomed Mater Res. 1996 Aug;31(4):545-54, previously cited 7/29/2022).
Claim 9 is drawn to a method for coating calcium phosphate particles with a peptide comprising:
Mixing a calcium phosphate particles with a first aqueous salt solution having an osmolarity value of between 400 and 1,200 mOsm and a pH of between 6.5 and 8.5 followed by drying the calcium phosphate particles;
Coating a peptide of SEQ ID NO: 1 (p-15) to the calcium phosphate particles from step (i) in a second aqueous salt solution having osmolarity value 400 and 1,200 mOsm and a pH of between 6.5 and 8.5;
Separating the coated calcium phosphate particles from the second aqueous salt solution and peptide binding to the pretreated particles is increased in comparison to peptide binding to calcium phosphate particles that are not pretreated with buffered saline solution (reading PBS).
Wu et al. teach one biocompatible and bioactive material often used as implant coating for bone regeneration is hydroxyapatite (HAP, Ca10(PO4)6(OH)2, a calcium phosphate nanoparticle), known in the art (p2452, Introduction, para 1). Wu et al. suggest the use of ubiquitous role of mineral (e.g., HAP)-protein interactions both in the design of biomedical implants. Wu et al. teach a method of making hydroxyapatite (HAP, Ca10(PO4)6(OH)2) nanoparticles (calcium phosphate particles) with controlled size, crystallinity, and shape were synthesized through a typical wet precipitation reaction followed by a drying step at 20°C (p2453, col 2, HAP Nanoparticle Synthesis).
Wu et al. did not teach beneficially using freeze drying for preparation of calcium phosphate nanoparticle before coating a bioactive peptide.
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Bohner et al. teach synthesis of calcium phosphate particles for dental and orthopedic applications (Title). Bohner et al. teach calcium phosphate particles including hydroxyapatites (e25103-1, col 1, para 1). Bohner et al. teach calcium phosphate particles based bone substitutes are available in different forms such as granules, porous blocks, cements, “putties” ( non-setting slurries or pastes), sponges/foams, or strips/membranes (e25103-1, col 2, para 2). Bohner et al. teach the advantage of using freeze drying method to make calcium phosphate particles to maintain the porous structure compared to other drying methods shown as follows (e25103-7, Fig 4). Thus, it would be beneficial to use freeze drying method to dry Wu’s calcium phosphate particles (e.g., hydroxyapatite) to maintain the porous structure of calcium phosphate particles before coating a peptide. Similarly, Benedict et al. teach bone mineral matrix (ABM), a calcium phosphate ceramic (reading on a calcium phosphate particle), coated with a biologically active peptide. Benedict et al. suggest the coated peptide of P-15 is a peptide fragment taken from Type I collagen and acts as a cell binding agent [0021] for bone repair (Abstract). Benedict et al. teach P-15 is able to recruit cells that are already destined to become bone cells (osteogenic) and cause them to lay down on the surface of the matrix [0023]. Benedict et al. further teach P-15 peptide coated on ABM particle [0024]. Benedict et al. suggest lyophilization has many advantages over simply air drying or vacuum drying ABM containing materials. Benedict et al. suggest freezing the material of calcium phosphate particles first, and then evaporating the water leaves many holes where the ice crystals sublime giving rise to a very porous structure. The porous structure allows cells, blood, and bone marrow easy access through the holes to the particles, suggesting also beneficial increase of coating area for P-15 peptide to adhere to the surface of porous structure after freeze drying. Benedict et al. teach if air drying and vacuum drying without freezing, the hydrogel (reading a scaffold) structure continues to collapse as the water evaporates, thus preventing the creation of a porous structure. Sublimation, rather than evaporation, is the key to creating the porous structure desired [0027], consistent with Bohner et al. (e25103-7, Fig 4). Thus, one of ordinary skill in the art would beneficially use freeze drying process comprising sublimation to substitute Wu’s procedure of drying calcium phosphate particles at 20°C taught by Bohner et al. and Benedict et al. before coating the P-15 peptide. Qian et al. is further cited to show the P-15 consisting of the elected peptide sequence of SEQ ID No: 1, GTPGPQGIAGQRGVV, (p545, col 2, Peptide synthesis).
Wu et al. in view of Bohner et al., Benedict et al., and Qian et al. do not specify beneficial use of osmotic pretreatment of the calcium phosphate particles prior to freeze drying.
Barbosa-Canovas is cited to show that osmotic pretreatment (hypertonic solution) a sample prior to freeze drying can beneficially reduce the drying time by 30% (p282, para 1). Barbosa-Canovas further teaches a hypertonic solution comprising sugar or salt is known as osmotic dehydration (p265, Introduction, para 1). Thus, one of ordinary skill in the art would have found it obvious to beneficial use a hypertonic salt solution for osmotic pretreatment of a calcium phosphate particle sample before freeze drying to reduce freeze drying time and energy cost of the freeze-drying process taught by Barbosa-Canovas.
Wu et al. in view of Bohner et al., Benedict et al., Qian et al., and Barbosa-Canovas do not specify a hypertonic salt solution suitable for osmotic pretreatment of calcium phosphate particles prior to freeze drying and also suitable for coating P-15 peptide after adding water for rehydration of the pre-treated and freeze-dried calcium phosphate particles. Natan et al. is cited to show common knowledge by adding pure water to rehydration of a freeze-dried sample well known in the art (See Methodology/Principal Findings in the abstract).
Behnam teaches bone matrix compositions and methods (Title). Behnam teaches a protein composition comprises hydroxyapatite or tricalcium phosphate (reading on calcium phosphate particle) and the protein can serve as a source of collagen type I [0082]. Behnam teaches the protein can further be permitted to absorb onto the mineral surface [0083], such as P-15 peptide coated calcium phosphate particles taught by Benedict et al. described above [0021, 0024]. Behnam teaches bone matrix compositions (including a protein coated hydroxyapatite) can be prepared at physiological pH approximately 7.2-8.0, or preferably 7.4-7.6 with osmotic pressure between 50-500 mosm/kg. The salt concentration may be approximately 100-300 mM NaCl [0088]. An aqueous solution comprises optimized osmotic pressure between 50-500 mosm/kg, 100-300 mM NaCl, at physiological pH approximately 7.2-8.0 can be beneficial used for (a) osmotic pretreatment (hypertonic solution) of Wu’s calcium phosphate particles before freeze drying to produce porous calcium phosphate particles (Bohner et al. and Barbosa-Canovas) and (b) rehydration of freeze-dried and pretreated calcium phosphate particles by adding pure water (See Natan et al. Abstract) to the freeze-dried calcium phosphate particles for coating the P-15 peptide.
Wu further teach buffer exchange by dialysis and decanting the supernatant to collect calcium phosphate particles (p2453, col 2, HAP Nanoparticle Synthesis). Thus, it would be obvious to use dialysis and decanting supernatant taught by Wu et al. to separate P-15 peptide coating buffer of the second aqueous salt solution from P-15 peptide coated calcium phosphate particles.
With respect to step (i) in claim 9, Wu et al. teach a method of making hydroxyapatite (HAP, Ca10(PO4)6(OH)2) nanoparticles (calcium phosphate particles) with controlled size, crystallinity, and shape were synthesized through a typical wet precipitation reaction for coating a protein (Title and Abstract; p2453, col 2, HAP Nanoparticle Synthesis) followed by a drying step at 20°C. Bohner et al. and Benedict et al. teach the advantage of using freeze drying method to make calcium phosphate particles to maintain the porous structure compared to other drying method (See Bohner et al. e25103-7, Fig 4 and Benedict et al. [0027]). The porous structure allows cells, blood, and bone marrow easy access through the holes to the particles [0027], suggesting beneficial increase of coating area for a peptide to adhere to the porous structure after freeze drying. Barbosa-Canovas is cited to show that osmotic pretreatment (hypertonic solution) a sample prior to freeze drying can beneficially reduce the drying time by 30% (p282, para 1). Behnam teaches bone matrix compositions (including a protein coated hydroxyapatite) can be prepared at physiological pH approximately 7.2-8.0, or preferably 7.4-7.6 with osmotic pressure between 50-500 mosm/kg. The salt concentration may be approximately 100-300 mM NaCl [0088]. One of ordinary skill in the art would at once envisage Behnam’s aqueous solution comprising osmotic pressure optimized between 50-500 mosm/kg, 100-300 mM NaCl, at physiological pH approximately 7.2-8.0 can be beneficial used for (a) osmotic pretreatment (hypertonic solution) of Wu’s calcium phosphate particles before freeze drying to produce pretreated and dried porous calcium phosphate particles (taught by Barbosa-Canovas).
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With respect to step (ii) in claim 9, Natan et al. teach adding pure water to rehydration of a freeze-dried sample (See Methodology/Principal Findings in the abstract); thus, one of ordinary skill in the art would have found it obvious by adding pure water to rehydrate pretreated and freeze-dried calcium phosphate particles (e.g., Benedict et al. claim 22) for coating Benedict’s P-15 peptide in a hypertonic solution optimized between 50-500 mosm/kg, 100-300 mM NaCl, at physiological pH approximately 7.2-8.0 suggested by Behnam [0088]. Although Benedict et al. or Behnam did not specify a particular buffer, one of ordinary skill in the art has common knowledge to select suitable buffers comprising Tris, TAPSO, HEPES, TES, MOPS buffer able to maintain pH 7.2-8.0 as taught by Will et al. shown as follows (p712, Table 1) for an intended purpose of pretreatment of calcium phosphate particles and coating a peptide to rehydrated calcium phosphate particles. Qian et al. is further cited to show the P-15 consisting of the elected peptide sequence of SEQ ID No: 1, GTPGPQGIAGQRGVV, (p545, col 2, Peptide synthesis).
With respect to step (iii) in claim 9, Wu further teach buffer exchange by dialysis and decanting the supernatant to collect calcium phosphate particles (p2453, col 2, HAP Nanoparticle Synthesis). Thus, it would be obvious to use dialysis and/or decanting supernatant taught by Wu et al. to separate P-15 peptide coating buffer of the second aqueous salt solution from P-15 peptide coated calcium phosphate particles.
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The use of Behnam’s hypertonic solution for pretreated calcium phosphate particles (e.g., hydroxyapatite) prior to freeze drying and rehydration of calcium phosphate particles with pure water (See Natan et al. Abstract) would have maintained porous structure of calcium phosphate particles for cell migration into it and one of ordinary skill in the art would expect the porous structure to provide more binding sites for the P-15 peptide binding to calcium phosphate particles (e.g., hydroxyapatite) suggested by Bohner’s figure 4 as follows. Behnam’s hypertonic solution is not buffered saline solution because it has much higher osmolarity and salt concentration than buffered saline solution.
One of ordinary skill in the art before the effective filing date of this invention would have found it obvious to substitute Wu’s method of drying calcium phosphate particles with freeze drying process taught by Benedict et al. and Barbosa-Canovas because (a) Benedict et al. suggest freezing the material of calcium phosphate particles first, and then evaporating the water leaves many holes where the ice crystals sublime giving rise to a very porous structure. The porous structure allows cells, blood, and bone marrow easy access through the holes to the particles, suggesting also beneficial increase of coating area for a peptide to adhere to the surface porous structure after freeze drying and (b) Barbosa-Canovas is cited to show that osmotic pretreatment (hypertonic solution) a sample prior to freeze drying can beneficially reduce the drying time by 30% (p282, para 1) and a hypertonic solution comprising sugar, salt is known as osmotic dehydration (p265, Introduction, para 1). The combination would have reasonable expectation of success because all references teach drying a sample.
One of ordinary skill in the art before the effective filing date of this invention would have found it obvious to combine (i) Wu et al. in view of Benedict et al. and Barbosa-Canovas and (ii) Behnam because (a) Wu et al. in view of Benedict et al. and Barbosa-Canovas teach osmotic pretreatment of a calcium phosphate particles with hypertonic solution prior to freeze drying can beneficially reduce the drying time by 30% (p282, para 1) and (b) Behnam teaches bone matrix compositions (including a protein coated hydroxyapatite) can be prepared at physiological pH approximately 7.2-8.0, or preferably 7.4-7.6 with osmotic pressure between 50-500 mosm/kg. The salt concentration may be approximately 100-300 mM NaCl [0088]. An hypertonic aqueous solution comprises osmotic pressure between 50-500 mosm/kg, 100-300 mM NaCl, at physiological pH approximately 7.2-8.0 can be beneficial used for (1) osmotic pretreatment (hypertonic solution) of Wu’s calcium phosphate particles before freeze drying to produce dried pretreated calcium phosphate particles (taught by Barbosa-Canovas) and (2) rehydration of freeze-dried pretreated calcium phosphate particles for coating the P-15 peptide. The combination would have reasonable expectation of success because both Barbosa-Canovas and Behnam teach the use of a hypertonic solution for treatment of samples. Qian et al. teach the coated peptide is P-15 consisting of the elected peptide sequence of SEQ ID No: 1, GTPGPQGIAGQRGVV, (p545, col 2, Peptide synthesis).
With respect to claim 10, the reaction time for coating Benedict’s P-15 peptide to Wu’s calcium phosphate particles is a result effective variable can be determined by routine experimentation depending on the concentration of Benedict’s P-15 peptide, Wu’s calcium phosphate particles, and temperature. Thus, one of ordinary skill in the art would optimize the coating time such as 2 hours, 3 hours, 5 hours, or 24 hours by routine experimentation. For example, Qian et al. teach the coating step comprising incubation of ABM/hydroxyapatite (calcium phosphate particle) with the peptide of P-15 in a coating solution for 24 hours (p546, col 1, Preparation of ABM.P-15).
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With respect to claim 11, one of ordinary skill in the art has common knowledge to select suitable buffers comprising Tris, TAPSO, HEPES, TES, MOPS buffer able to maintain pH 7.2-8.0 as taught by Will et al. shown as follows (p712, Table 1) for an intended purpose of pretreatment of calcium phosphate particles and coating a peptide to rehydrated calcium phosphate particles.
With respect to claim 12, Behnam teaches the salt concentration may be approximately 100-300 mM NaCl [0088].
With respect to claim 39, Benedict et al. and Barbosa-Canovas teach the use of osmotic pretreatment (hypertonic solution) followed by freezing drying to make dry calcium phosphate particles. See rejection of claim 9 in details above.
With respect to claim 40, the reaction time for coating Benedict’s P-15 peptide to Wu’s calcium phosphate particles is a result effective variable can be determined by routine experimentation depending on the concentration of Benedict’s P-15 peptide, Wu’s calcium phosphate particles, and temperature. Thus, one of ordinary skill in the art would optimize the coating time such as 2 hours, 3 hours, 5 hours, or 24 hours by routine experimentation. For example, Qian et al. teach the coating step comprising incubation of ABM/hydroxyapatite (calcium phosphate particle) with the peptide of P-15 in a coating solution for 24 hours (p546, col 1, Preparation of ABM.P-15). See rejection of claim 9 in details above.
With respect to claim 41, one of ordinary skill in the art has common knowledge to select suitable buffers comprising Tris, TAPSO, HEPES, TES, MOPS buffer able to maintain pH 7.2-8.0 as taught by Will et al. (p712, Table 1) for an intended purpose of pretreatment of calcium phosphate particles and coating a peptide to rehydrated calcium phosphate particles. Also, see rejection of claim 11 above.
With respect to claim 42, Behnam teaches the salt concentration may be approximately 100-300 mM NaCl [0088].
Applicant’s Arguments
Due to the New Ground of Rejection with a new reference, relevant arguments are listed as follows.
Applicant respectfully disagrees and notes that this interpretation of Behnam conflates the "demineralized bond matrix scaffold" taught by Behnam [0128-0129] (Remarks, p10, para 2-5].
Applicant asserts that Behnam's conditions for preparing demineralize bone provide no useful teaching to one of skill in the art interested in coating calcium phosphate particles with a peptide (Remarks, p11, para 2).
Nowhere in Benedict is it taught or suggested to pretreat the ABM particles to improve their adhesion to peptides.
The amendments of a first and a second aqueous salt solutions having an osmolarity value of between 400 and 1,200 mOsm at pH 6.5-8.5 to increase peptide binding to calcium phosphate particles are not obvious to the cited prior art references.
Response to Arguments
Applicant's arguments filed 4/23/2025 have been fully considered but they are not persuasive for the reasons as follows.
Applicant’s argument (i) is not persuasive because (A) Behnam's teach a protein composition comprising hydroxyapatite (calcium phosphate particles) [0082-0083] not limited to demineralized bone as argued by applicant and (B) the rejection is based on hypertonic salt solution taught by Behnam not "demineralized bond matrix scaffold" as argued by applicant.
Applicant’s argument (ii) is not persuasive because Behnam’s hypertonic salt solution is very relevant for osmotic pretreatment (hypertonic solution) for a sample of calcium phosphate particles prior to freeze drying can beneficially reduce the drying time by 30% as suggested by Barbosa-Canovas (p282, para 1). Furthermore, Behnam’s hypertonic salt solution is also very relevant for rehydration of pretreated and freeze-dried calcium phosphate particles for coating the P-15 peptide. "The use of patents as references is not limited to what the patentees describe as their own inventions or to the problems with which they are concerned. They are part of the literature of the art, relevant for all they contain." In re Heck, 699 F.2d 1331, 1332-33, 216 USPQ 1038, 1039 (Fed. Cir. 1983). SEE MPEP 2123(I).
Applicant’s argument (iii) is not persuasive because Benedict et al. suggest freezing the material of calcium phosphate particles first, and then evaporating the water leaves many holes where the ice crystals sublime giving rise to a very porous structure. The porous structure allows cells, blood, and bone marrow easy access through the holes to the particles, suggesting beneficial increase of coating area for a peptide to adhere to the porous structure after freeze drying. A reference may be relied upon for all that it would have reasonably suggested to one having ordinary skill in the art, including nonpreferred embodiments. Merck & Co. v. Biocraft Labs., Inc. 874 F.2d 804, 10 USPQ2d 1843 (Fed. Cir. 1989), cert. denied, 493 U.S. 975 (1989).
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SEE MPEP 2123(I). Furthermore, Bohner et al. teach the advantage of using freeze drying method to make calcium phosphate particles to main the porous structure compared to other drying methods shown as follows (e25103-7, Fig 4). A larger peptide contacting surface of a freeze-dried porous calcium phosphate particles is expected to increase peptide adhesion to the hypertonic salt solution pretreated and freeze-dried porous calcium phosphate particles.
Applicant’s argument (iv) is not persuasive because of the reasons as follows.
(a) One of ordinary skill in the art need not see the identical problem addressed in a prior art reference to be motivated to apply its teachings. See MPEP 2144(IV) Rationale different from applicant’s is permissible.
(b) Barbosa-Canovas is cited to show that osmotic pretreatment (hypertonic solution) a sample prior to freeze drying can beneficially reduce the drying time by 30% (p282, para 1). Behnam teaches bone matrix compositions (including a protein coated hydroxyapatite) can be prepared at physiological pH approximately 7.2-8.0, or preferably 7.4-7.6 with osmotic pressure between 50-500 mosm/kg. The salt concentration may be approximately 100-300 mM NaCl [0088]. An aqueous solution comprises osmotic pressure between 50-500 mosm/kg, 100-300 mM NaCl, at physiological pH approximately 7.2-8.0 can be beneficial used for (1) osmotic pretreatment (hypertonic solution) of Wu’s calcium phosphate particles before freeze drying to produce dried pretreated calcium phosphate particles (taught by Barbosa-Canovas) and (2) rehydration of freeze-dried pretreated calcium phosphate particles for coating the P-15 peptide. The expectation of some advantage is the strongest rationale for combining references. See MPEP 2144(II).
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
Claims 9-12 and 39-42 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 5, and 16 of U.S. Patent No. 9,415,139 B2 (the ‘139 patent) in view of Wu et al., Bohner et al., Benedict et al., Barbosa-Canovas, Natan et al., Behnam, Will et al. and Qian et al.
Claims 1 and 5 of the ‘139 patent disclosed hydroxyapatite particles (calcium phosphate particles) coated with P-15 peptide.
Claim 16 of the ‘139 patent disclosed P-15 peptide sequence of SEQ ID NO: 1.
Claims 1, 5, and 16 of the ‘139 patent do not explicitly teach a method of making P-15 coated hydroxyapatite particles (calcium phosphate particles).
The relevancy of Wu et al., in view of Bohner et al., Benedict et al., Barbosa-Canovas, Natan et al., Behnam, Will et al., and Qian et al. as applied to claims 9-12 and 39-42 not repeated here.
Because Wu et al., in view of Bohner et al., Benedict et al., Barbosa-Canovas, Natan et al., Behnam, Will et al., and Qian et al. teach beneficial use of a hypertonic solution for pretreatment of calcium phosphate particles before freeze drying and rehydration of freeze-dried calcium phosphate particles with pure water for coating P-15 peptide, one of ordinary skill in the art would have found it obvious to combine claims 1, 5, and 16 of the ‘139 patent with Wu et al., in view of Bohner et al., Benedict et al., Barbosa-Canovas, Natan et al., Behnam, Will et al., and Qian et al.
Thus, claims 1, 5, and 16 of the ‘139 patent in view of Wu et al., Bohner et al., Benedict et al., Barbosa-Canovas, Behnam, and Qian et al. are obvious to the instant claims 9-12 and 39-42.
Conclusion
No claim is allowed.
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/J.L/Examiner, Art Unit 1658
12-September-2025
/LI N KOMATSU/Primary Examiner, Art Unit 1658