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 .
DETAILED ACTION
RESPONSE TO AMENDMENT
Status of Application/Amendments/claims
2. Applicant’s amendment filed April 23, 2026, July 10, 2026 and July 30, 2026 is acknowledged. Claims 1-14, 21 and 23-24 are canceled. Claims 18-20 and 22 are amended. Claims 15-20 and 22 are pending in this application. Claims 15-17 are withdrawn with traverse (filed 09/17/2025) from further consideration pursuant to 37 CFR 1.142(b), as being drawn to a nonelected invention, there being no allowable generic or linking claim. Applicant timely traversed the restriction (election) requirement in the reply filed on September 17, 2025.
3. Claims 18-20 and 22 are under examination with respect to SEQ ID NOs: 4 and 7 and Wilson’s disease in this office action.
4. Applicant’s arguments filed on April 23, 2026, July 10, 2026 and July 30, 2026 have been fully considered but they are not deemed to be persuasive for the reasons set forth below.
Drawings
5. The drawings were received on April 23, 2026. These drawings are acceptable. Thus, the objection to figures 3-4 is withdrawn.
Claim Rejections/Objections Withdrawn
6. The objection to claims 15-17 is withdrawn in response to Applicant’s amendment to the claims.
The rejection of claim 20 under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite is withdrawn in response to Applicant’s amendment to the claim.
Claim Rejections/Objections Maintained
In view of the amendment filed on April 23, 2026, July 10, 2026 and July 30, 2026, the following rejections are maintained.
Claim Rejections - 35 USC § 112
7. The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Claims 18-20 and 22 stand rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, because the specification, while being enabling for partially restoring myelination from Copper overexposure-induced myelination damage, increasing reduced GFP expression levels caused by Copper overexposure and decreasing increased heart rates caused by Copper overexposure in an animal model of Copper-induced demyelination, zebrafish transformant (i.e. mGFP transgenic) treated with 4uM Copper, by administering a copper oxidase peptide CP001 (SEQ ID NO:3), CP002 (SEQ ID NO:4) or CP002s (SEQ ID NO:7) to the animal model of copper-induced demyelination (zebrafish transformant treated with 4uM Copper) as compared to the animal model with no treatment, does not reasonably provide enablement for a method for alleviating or treating all forms of disease associated with copper-induced demyelination by a composition comprising one or more of peptides each consisting of an amino acid sequence set forth in SEQ ID NO: 4 or 7 as broadly claimed. The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to use the invention commensurate in scope with these claims. The rejection is maintained for the reasons of record and the reasons set forth below.
Claims 18-20 and 22 as amended are drawn to a method for alleviating or treating a disease associated with copper-induced demyelination, comprising administering to a subject in need thereof a composition comprising one or more of peptides, each consisting of an amino acid sequence set forth in SEQ ID NO: 4 or 7.
Briefly, the specification only discloses administration of a copper oxidase peptide CP001 (SEQ ID NO:3), CP002 (SEQ ID NO:4) or CP002s (SEQ ID NO:7) at a concentration of 5uM or 10uM to an animal model of copper overexposure-induced demyelination, zebrafish transformant (i.e. mGFP transgenic) resulted in partially restoring myelination from Copper-induced myelination damage, increasing the GFP expression levels reduced by Copper overexposure, and decreasing the heart rate increased by Copper overexposure in the animal model of copper-induced demyelination, zebrafish transformant (i.e. mGFP transgenic) treated with 4uM Copper when compared to the animal model with no treatment or treated with a therapeutic agent for Wilson’s disease, DPA (penicillamine/D-Penicillamine) or TETA (trientine/Trientine) (Examples 5-9, Figures 7-11).
The specification provides no well-established structural and functional relationship or correlation between partially restoring myelination from myelination damage caused by Copper-overexposure, restoring GFP expression that is reduced by Copper-overexposure and restoring heart rates from increased heart rates caused by Copper-overexposure in an animal model of copper overexposure-induced demyelination in zebrafish transformant (i.e. mGFP transgenic) treated with 4uM Copper by the peptide CP001 (SEQ ID NO:3), CP002 (SEQ ID NO:4) or CP002s (SEQ ID NO:7) and the pathogeneses or causes of all forms of diseases associated with copper-induced demyelination including multiple sclerosis (MS), Alzheimer’s disease (AD) and Wilson’s diseases caused by different mechanisms or other mechanisms by a composition comprising one or more of peptides, each consisting of an amino acid sequence set forth in SEQ ID NO: 4 or 7.
There is no well-established correlation between the animal model of copper overexposure-induced demyelination in zebrafish transformant treated with 4uM Copper and the pathogeneses or causes of all forms of diseases associated with copper-induced demyelination including MS, AD, and Wilson’s diseases caused by different mechanism or other mechanisms in vivo in view of Falkenburger et al. (see p. summary Falkenburger et al., J. Neural. Transm, 2006; 70:261-268, cited previously), Tayebati (see p. 106, 1st col, 2nd paragraph, Tayebati, Mech. Ageing Dev. 2006. 127: 100-8, cited previously) and Sarter (see p. 645, abstract, Sarter, Neurosci. and Biobehav. Rev. 2004. 28: 645-650, cited previously).
The animal model of copper overexposure-induced demyelination in zebrafish transformant (i.e. mGFP transgenic) treated with 4uM Copper does not have any genetic deficits. However, Wilson’s disease is an inherited autosomal recessive disorder caused by a mutation of the APT7B gene that prevents the body from eliminating excess copper, which has a genetic deficit. The specification fails to provide sufficient support to demonstrate that Wilson’s disease caused by a mutation of the APT7B gene that prevents the body from eliminating excess copper can be treated by the claimed peptides of SEQ ID NO:4 or 7 or the claimed peptide consisting of an amino acid sequence set forth in SEQ ID NO: 4 or 7. The specification fails to provide sufficient support to demonstrate that MS or AD caused by different mechanisms can be treated by the claimed peptides of SEQ ID NO:4 or 7 or the claimed peptide consisting of an amino acid sequence set forth in SEQ ID NO: 4 or 7. The specification fails to teach what other diseases are associated with copper-induced demyelination and whether all forms of diseases associated with copper-induced demyelination can be treated by the claimed composition comprising one or more of peptides, each consisting of an amino acid sequence set forth in SEQ ID NO: 4 or 7.
Thus, it is unpredictable whether administration of the claimed composition can alleviate or treat all forms of diseases associated with copper-induced demyelination including MS, AD and Wilson’s disease, indicating that undue experimentation is required by a skilled artisan to perform while practicing the full scope of the claimed invention.
The specification also fails to provide a structural and functional relationship between the peptide CP001 (SEQ ID NO:3), CP002 (SEQ ID NO:4) or CP002s (SEQ ID NO:7) and the peptide consisting of an amino acid sequence set forth in SEQ ID NO: 4 or 7, which includes fragments with SEQ ID NO:4 or 7 in partially restoring myelination from myelination damage caused by Copper-overexposure, restoring GFP expression from reduced GFP expression caused by Copper-overexposure and restoring heart rates from increased heart rates caused by Copper-overexposure in an animal model of copper overexposure-induced demyelination in zebrafish transformant treated with 4uM Copper or even in treating all forms of diseases associated with copper-induced demyelination including MS, AD and Wilson’s diseases caused by different mechanisms or other mechanisms. The specification fails to teach what other amino acid sequences, structures and features can or cannot be changed or included in the claimed peptide consisting of an amino acid sequence set forth in SEQ ID NO: 4 or 7 including fragments within SEQ ID NO:4 or 7. Thus, it is unpredictable whether administration of the claimed composition can alleviate or treat all forms of diseases associated with copper-induced demyelination including MS, AD and Wilson’s disease, indicating that undue experimentation is required by a skilled artisan to perform while practicing the full scope of the claimed invention.
Therefore, in view of the breadth of the claims, the lack of guidance in the specification, the limited examples, the unpredictability of inventions, and the current status of the art, undue experimentation would be required by one of skill in the art to perform in order to practice the full scope of the claimed invention as it pertains to a method for alleviating or treating a disease associated with copper-induced demyelination by administering to a subject in need thereof a composition comprising one or more of peptides, each consisting of an amino acid sequence set forth in SEQ ID NO: 4 or 7.
Response to Arguments
On p. 7-9 of the response, Applicant argues that: i) the claimed composition comprising CP004 (SEQ ID NO:4) and CP002s (SEQ ID NO:7) were confirmed in an animal model confirmed to partially restore myelin damage caused by excessive copper exposure, increase GFP expression levels reduced by excessive copper and decrease elevated heart rate. ii) Wilson disease, MS and AD have been reported to have excessive copper exposure and resulting demyelination. Applicant further cites Dusek et al. (Annals of transl. med. 2019, 7: S64), Brewer (Copper in Wilson’s and Alzheimer’s diseases, copper-lowering therapy in cancer and other diseases, and copper deficiency: Molecular,Genetic, and Nutritional Aspects of Major and Trace Minerals, Academic Press, 2017; 115-129), Depp et al. (Nature, 2023; 618, 7964:349-357), Deepika et al. (Biometals, 2025; 38.5: 1381-1420) and Hou et al. (Trans. Res. 2008; 152.5:239-244) in support of the arguments.
Applicant's arguments have been fully considered but they are not found persuasive. The references of Dusek, Brewer, Depp, Deepika and Hou are noted. Contrary to Applicant's arguments, the examiner asserts that based on MPEP §2164, MPEP §§2164.01-2164.06(b) & 2164.08, neither the specification nor the prior art provides sufficient guidance to enable a skilled artisan to practice the full scope of the claimed invention without undue experimentation because of the following:
i. The data from the specification only showed that: administration of a copper oxidase peptide CP001 (SEQ ID NO:3), CP002 (SEQ ID NO:4) or CP002s (SEQ ID NO:7) at a concentration of 5uM or 10uM to an animal model of copper overexposure-induced demyelination, zebrafish transformant (i.e. mGFP transgenic) resulted in partially recovering myelination from Copper-induced myelination damage, increasing GFP expression levels reduced by Copper overexposure, and decreasing heart rates increased by Copper overexposure in the animal model of copper-induced demyelination, zebrafish transformant (i.e. mGFP transgenic) treated with 4uM Copper when compared to the animal model with no treatment.
The cited references of Dusek, Brewer, Depp, Deepika and Hou fail to provide support to demonstrate that administration of the claimed peptides can alleviate or treat all forms of diseases associated with copper-induced demyelination including MS, AD and Wilson’s disease. Copper-induced myelination damage is not the only cause of Wilson’s disease, MS or AD.
ii. The animal model of copper overexposure-induced demyelination in zebrafish transformants (i.e. mGFP transgenic) treated with 4uM Copper is not an art accepted animal model for Wilson’s diseases as taught by Reed et al. (J. Neurochem. 2018;146:356-373) because the zebrafish transformant with a mGFP transgene used in Examples of instant specification does not have any genetic deficits in APT7B gene or a mutation of the APT7B gene that prevents the body from eliminating excess copper. The specification provides insufficient guidance to demonstrate that administration of the claimed composition comprising one or more peptides each consisting of an amino acid sequence set forth in SEQ ID NO: 4 or 7 can treat Wilson’s disease because Wilson’s disease is caused by a mutation of the APT7B gene that prevents the body from eliminating excess copper, which is different from a normal zebrafish transformant temporarily exposed to excessive Copper.
The animal model of copper overexposure-induced demyelination in zebrafish transformant (i.e. mGFP transgenic) treated with 4uM Copper is not an art accepted animal model for MS as taught by Sujitha et al. (Meta. Brain Dis. 2026; 41:67. Doi.org/10.1007/s11011-026-01837-5). The specification provides insufficient guidance to demonstrate that administration of the claimed composition comprising one or more peptides each consisting of an amino acid sequence set forth in SEQ ID NO: 4 or 7 can treat MS because MS is an autoimmune disease and myelination damage caused by Copper overexposure is not the only cause of MS. There is no nexus between collective immune-mediated demyelination in MS and the copper overexposure-induced demyelination in zebrafish transformant (i.e. mGFP transgenic) treated with 4uM Copper. There is also no correlation between the treatment of the claimed peptides in progressive demyelination associated with CD4+ T cells infiltration specific to MOG or genes involved in the pathogenesis of MS, or other mechanisms or genes associated with MS. Thus, it is unpredictable whether administration of the claimed peptide composition can treat MS, indicating undue experimentation is required by a skilled artisan to perform while practicing the claimed method of treating MS.
The animal model of copper overexposure-induced demyelination in zebrafish transformant (i.e. mGFP transgenic) treated with 4uM Copper is not an art accepted animal model for AD as taught by Tayebati (see p. 106, 1st col, 2nd paragraph, Tayebati, Mech. Ageing Dev. 2006. 127: 100-8) and Sarter (see p. 645, abstract, Sarter, Neurosci. and Biobehav. Rev. 2004. 28: 645-650). The molecular mechanisms underlying the cognitive dysfunction or dementia of AD are unclear (see p. 94; Henstridge et al. Nat. Rev. Neurosci. 2019; 20: 94-107, cited previously). The specification provides insufficient guidance to demonstrate that administration of the claimed composition comprising one or more peptides each consisting of an amino acid sequence set forth in SEQ ID NO: 4 or 7 can treat AD or cognitive dysfunction or dementia in AD because myelination damage caused by Copper overexposure is not the only cause of cognitive dysfunction or dementia in AD. Several factors and genes are involved in pathogenesis of AD including ageing, inflammation and immune response, APP, presenilin1/2, ApoE and genes involved in the amyloid cascade, genes involved in the mitochondrial cascade as taught by Swerdlow (p. 348-344, Swerdlow, Clin. Interv. Ageing 2007; 2:347-359, cited previously), Atwood et al. (p. abstract; Atwood et al., J. Alzheimer’s Disease; 2015; 47:33-47, cited previously) and Henstridge et al. (p. 95-103; Henstridge et al., Nat. Rev. Neurosci. 2019; 20: 94-107, cited previously).
There is no correlation between copper overexposure-induced demyelination in zebrafish transformant (i.e. mGFP transgenic) treated with 4uM Copper and Ab pathology or other genes involved in the amyloid cascade, genes involved in the mitochondrial cascade or in AD pathology (see p. 106, 1st col, 2nd paragraph, Tayebati. Mech. Ageing Dev. 2006. 127: 100-8, cited previously). The minimum criteria for an animal model to evaluate treatment of AD require the presence of both of Abeta pathology and tau pathology in an animal model and also require detection of both Abeta pathology and tau pathology by using an A11 antibody for detection of oligomeric Abeta, an 4G8 antibody for detection of aggregated Abeta, an AT8 antibody for detection of hyperphosphorylated tau and an AT100 antibody for detection of aggregated tau as evidenced by Gotz et al. (see p. 584-585, box 1-2, Gotz et al. Nat. Rev. Neurosci. 2018; 19: 583-598). However, the data from the copper overexposure-induced demyelination in zebrafish transformant (i.e. mGFP transgenic) treated with 4uM Copper only showed partially recovering myelination from Copper-induced myelination damage, increasing GFP expression levels reduced by Copper overexposure, and decreasing an increased heart rate caused by Copper overexposure in the animal model of copper-induced demyelination, zebrafish transformant (i.e. mGFP transgenic) treated with 4uM Copper when compared to the animal model with no treatment. There is no nexus between collective Abeta and Tau pathology in AD and the copper overexposure-induced demyelination in zebrafish transformant (i.e. mGFP transgenic) treated with 4uM Copper. There is also no correlation between the treatment of the claimed peptides in A pathology or genes involved in the pathogenesis of AD that is caused by A pathology, or other mechanisms or genes associated with AD. Thus, it is unpredictable whether administration of the claimed peptide composition can treat AD, indicating undue experimentation is required by a skilled artisan to perform while practicing the claimed method of treating AD.
Note that the scope of the claims must bear a reasonable correlation with the scope of enablement (In re Fisher, 166 USPQ 19 24 (CCPA 1970)). Without such guidance, it is not known what other diseases associated with copper-induced demyelination are, and it is unpredictable whether Wilson’s disease, MS and AD can be treated by the claimed peptide composition; and thus the experimentation left to those skilled in the art is extensive and undue. See Ex parte Forman, 230 USPQ 546 (Bd. Pat. App. & Int. 1986). Thus, the skilled artisan cannot readily know how to use the claimed invention as currently claimed without further undue experimentation. In re Marzocchi, 439 F.2d 220, 223-24, 169 USPQ 367, 369-70 (CCPA 1971)” See MPEP § 2164.03.
Therefore, in view of the breadth of the claims, the lack of guidance in the specification, limited working examples, the unpredictability of inventions, and the current status of the art, undue experimentation would be required by a skilled artisan to perform in order to practice the claimed invention as it pertains to a method for alleviating or treating a disease associated with copper-induced demyelination including MS, AD and Wilson’s disease by administering to the subject the claimed composition comprising one or more peptides each consisting of an amino acid sequence set forth in SEQ ID NO:4 or 7.
Accordingly, the rejection of claims 18-20 and 22 under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, lack of scope of enablement is maintained.
Claim Rejections - 35 USC § 112
8. Claims 18-20 and 22 stand ejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for pre-AIA the inventor(s), at the time the application was filed, had possession of the claimed invention. The rejection is maintained for the reasons of record and the reasons set forth below.
Briefly, claims 18-20 and 22 as amended encompass using one or more peptides, each consisting of an amino acid sequence of SEQ ID NO: 4 or 7 for alleviating or treating a genus of a disease associated with copper-induced demyelination. Applicant has not disclosed sufficient species of using the claimed peptides including fragments within SEQ ID NO:4 or 7 for alleviating or treating the broad genus of diseases associated with copper-induced demyelination.
The specification fails to provide sufficient support to demonstrate that Applicant is in possession of the claimed method. The specification provides no well-established structural and functional relationship or correlation between treatment of diseases associated with copper-induced demyelination by the claimed peptides including fragments within SEQ ID NO:4 or 7 and partially restoring myelination from Copper-induced myelination damage, increasing GFP expression reduced by Copper overexposure, and decreasing heart rate increased by Copper overexposure in the animal model of copper-induced demyelination, zebrafish transformant (i.e. mGFP transgenic) by CP001 (SEQ ID NO:3), CP002 (SEQ ID NO:4) or CP002s (SEQ ID NO:7) at a concentration of 5uM or 10uM, when compared to the animal model with no treatment. The specification provides no well-established structural and functional relationship or correlation between the animal model of copper-induced demyelination, zebrafish transformant (i.e. mGFP transgenic) and Wilson’s disease because Wilson’s disease is caused by a mutation of the APT7B gene that prevents the body from eliminating excess copper. But the animal model of copper-induced demyelination, zebrafish transformant (i.e. mGFP transgenic) does not have any genetic deficits, and is only temporally exposed to excessive copper. There is no well-established structural and functional relationship or correlation between the animal model of copper-induced demyelination, zebrafish transformant (i.e. mGFP transgenic) and MS because MS is an autoimmune disease leading to demyelination and Copper-induced demyelination is not the only cause. There is no well-established structural and functional relationship or correlation between the animal model of copper-induced demyelination, zebrafish transformant (i.e. mGFP transgenic) and AD because myelination damage caused by Copper overexposure is not the only cause of cognitive dysfunction or dementia in AD, and several factors and genes are involved in pathogenesis of AD including ageing, inflammation and immune response, APP, presenilin1/2, ApoE and genes involved in the amyloid cascade, genes involved in the mitochondrial cascade.
Response to Arguments
On p. 9-10 of the response, Applicant argues that i) the rejection has been overcome in view of amendment to the claims; ii) the specification provides support to demonstrate that Applicant is in possession of the claimed method and cites Examples 5, 8-9 and Figures 7-8 and 10-11 in support of the arguments.
Applicant's arguments have been fully considered but they are not found persuasive. Contrary to Applicant's arguments, the examiner asserts that based on MPEP §2163, MPEP §§2163.01-2163.03, the specification fails to provide sufficient description or information or evidence to demonstrate that Applicant is in possession of using the claimed peptides, each consisting of an amino acid sequence of SEQ ID NO: 4 or 7 for alleviating or treating a genus of a disease associated with copper-induced demyelination because:
i. There is no well-established structural and functional relationship or correlation between partially restoring myelination from myelination damage caused by Copper-overexposure, restoring GFP expression that is reduced by Copper-overexposure and restoring heart rates from increased heart rates caused by Copper-overexposure in an animal model of copper overexposure-induced demyelination in zebrafish transformant (i.e. mGFP transgenic) treated with 4uM Copper by the peptide CP001 (SEQ ID NO:3), CP002 (SEQ ID NO:4) or CP002s (SEQ ID NO:7) and the pathogeneses or causes of all forms of diseases associated with copper-induced demyelination including multiple sclerosis (MS), Alzheimer’s disease (AD) and Wilson’s diseases caused by different mechanisms or other mechanisms by a composition comprising one or more of peptides, each consisting of an amino acid sequence set forth in SEQ ID NO: 4 or 7 including fragments with SEQ ID NO:4 or 7.
ii. There is no well-established structural and functional relationship or correlation between the animal model of copper-induced demyelination, zebrafish transformant (i.e. mGFP transgenic) and Wilson’s disease because Wilson’s disease is caused by a mutation of the APT7B gene that prevents the body from eliminating excess copper. But the animal model of copper-induced demyelination, zebrafish transformant (i.e. mGFP transgenic) does not have any genetic deficits, and is only temporally exposed to excessive copper.
There is no well-established structural and functional relationship or correlation between the animal model of copper-induced demyelination, zebrafish transformant (i.e. mGFP transgenic) and MS because MS is an autoimmune disease leading to demyelination and Copper-induced demyelination is not the only cause.
There is no well-established structural and functional relationship or correlation between the animal model of copper-induced demyelination, zebrafish transformant (i.e. mGFP transgenic) and AD because myelination damage caused by Copper overexposure is not the only cause of cognitive dysfunction or dementia in AD, and several factors and genes are involved in pathogenesis of AD including ageing, inflammation and immune response, APP, presenilin1/2, ApoE and genes involved in the amyloid cascade, genes involved in the mitochondrial cascade.
The specification fails to teach what other diseases associated with copper-induced demyelination are and thus can be treated by the claimed peptides including fragments within SEQ ID NO:4 or 7.
The specification provides no well-established structural and functional relationship or correlation between treatment of diseases associated with copper-induced demyelination by the claimed peptides including fragments within SEQ ID NO:4 or 7 and partially restoring myelination from myelination damage caused by Copper-overexposure, restoring GFP expression that is reduced by Copper-overexposure and restoring heart rates from increased heart rates caused by Copper-overexposure in an animal model of copper overexposure-induced demyelination in zebrafish transformant (i.e. mGFP transgenic) treated with 4uM Copper by the peptide CP001 (SEQ ID NO:3), CP002 (SEQ ID NO:4) or CP002s (SEQ ID NO:7).
Since the common characteristics/features of other peptides including fragments within SEQ ID NO:4 or 7 are unknown and their effects on diseases associated with copper-induced demyelination including Wilson’s disease, MS and AD are also unknown, a skilled artisan cannot envision the functional correlations of the genus with the claimed invention.
Accordingly, in the absence of sufficient recitation of distinguishing identifying characteristics, the specification does not provide adequate written description of using the claimed genus of peptides including fragments within SEQ ID NO:4 or 7 for treating the genus of diseases associated with copper-induced demyelination.
Based on MPEP § 2161.01 and §2163, “to satisfy the written description requirement, a patent specification must describe the claimed invention in sufficient detail that one skilled in the art can reasonably conclude that the inventor had possession of the claimed invention. See, e.g., Moba, B.V. v. Diamond Automation, Inc., 325 F.3d 1306, 1319, 66 USPQ2d 1429, 1438 (Fed. Cir. 2003); Vas-Cath, Inc. v. Mahurkar, 935 F.2d at 1563, 19 USPQ2d at 1116”.
Vas-Cath Inc. v. Mahurkar, 19USPQ2d 1111, clearly states “applicant must convey with reasonable clarity to those skilled in the art that, as of the filing date sought, he or she was in possession of the invention. The invention is, for purposes of the ‘written description’ inquiry, whatever is now claimed.” (See page 1117.) The specification does not “clearly allow persons of ordinary skill in the art to recognize that [he or she] invented what is claimed.” (See Vas-Cath at page 1116).
As discussed above, the skilled artisan cannot envision the detailed chemical structure of the encompassed genus peptides including fragments within SEQ ID NO:4 or 7 for treating the genus of diseases associated with copper-induced demyelination, and therefore conception is not achieved until reduction to practice has occurred, regardless of the complexity or simplicity of the method of isolation. Adequate written description requires more than a mere statement that it is part of the invention and reference to a potential method of isolating it. The compound itself is required. See Fiers v. Revel, 25 USPQ2d 1601 at 1606 (CAFC 1993) and Amgen Inc. v. Chugai Pharmaceutical Co. Ltd., 18 USPQ2d 1016. One cannot describe what one has not conceived. See Fiddes v. Baird, 30 USPQ2d 1481 at 1483 and Centocor v. Abbott, 636 F.3d1341 (Fed. Cir. 2011) and AbbVie v. Janssen, 759 F.3d 1285 (Fed. Cir.2014). One cannot describe what one has not conceived. See Fiddes v. Baird, 30 USPQ2d 1481 at 1483.
Therefore, the claimed method has not met the written description provision of 35 U.S.C. §112, first paragraph. Applicant is reminded that Vas-Cath makes clear that the written description provision of 35 U.S.C. §112 is severable from its enablement provision (see page 1115). Applicant is directed to the Guidelines for the Examination of Patent Applications Under the 35 U.S.C. 112, ¶ 1 "Written Description" Requirement. See MPEP § 2161.01 and 2163.
Accordingly, the rejection of claims 18-20 and 22 under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement is maintained.
Conclusion
9. NO CLAIM IS ALLOWED.
Sequence alignments
SEQ ID NO:2 1019 GKWLLHCHVDDHIIGGMSAIY 1039
SEQ ID NO:4 (CP002; aa1019-1039) 1 GKWLLHCHVDDHIIGGMSAIY 21
SEQ ID NO:7 (CP002S; aa1024-1035) 1024 -----HCHVDDHIIGGM---- 1035
SEQ ID NO:3 (CP001; aa324-344) 1 GSWLVKCHVHDHYVGGMETLL 21
10. The prior art made of record and not relied upon is considered pertinent to applicant's disclosure.
Jung et al. (WO2024225597, published Oct 31, 2024, priority Apr 27, 2023; post-filing reference) teach an O minor ceruloplasmin multicopper oxidase 1 domain mutant peptide comprising the sequence of SEQ ID NO:4 or 7, which meets the limitation “a peptide represented by an amino acid sequence shown in SEQ ID NO:7”(see the sequence alignment below).
SEQ ID NO:4
BQE33274
(NOTE: this sequence has 2 duplicates in the database searched)
ID BQE33274 standard; peptide; 12 AA.
XX
AC BQE33274;
XX
DT 12-DEC-2024 (first entry)
XX
DE O. minor ceruloplasmin multicopper oxidase 1 domain mutant peptide SEQ:4.
XX
KW CP protein; Ceruloplasmin; alzheimers disease; encephalomyelitis; food;
KW huntingtons chorea; iron metabolism disorder; motor neurone disease;
KW movement disorder; multiple sclerosis; mutein; neurological disease;
KW neuromyelitis optica; neuroprotective; optic neuritis; paresthesia;
KW parkinsons disease; prion infection; prophylactic to disease;
KW protein therapy; therapeutic; wilson disease.
XX
OS Callistoctopus minor.
OS Synthetic.
XX
FH Key Location/Qualifiers
FT Misc-difference 2
FT /note= "Wild-type Cys substituted by His"
FT Modified-site 12
FT /note= "C-terminal amide"
XX
CC PN WO2024225597-A1.
XX
CC PD 31-OCT-2024.
XX
CC PF 05-MAR-2024; 2024WO-KR002774.
XX
PR 27-APR-2023; 2023KR-00055716.
XX
CC PA (KOAD ) NAT MARINE BIODIVERSITY INST KOREA.
XX
CC PI Jung SH, Lee JH, Jo SM, Kim HB, An HS;
XX
DR WPI; 2024-B52848/091.
XX
CC PT New peptide comprising specific amino acid sequences used in preparing
CC PT medicine or health functional food composition for preventing, improving
CC PT or treating nervous system disease including multiple sclerosis,
CC PT Parkinsons disease, Alzheimers disease, Menkes disease and/or Wilsons
CC PT disease.
XX
CC PS Claim 1; SEQ ID NO 4; 41pp; Korean.
XX
CC The present invention relates to novel peptides derived from
CC ceruloplasmin shown as SEQ ID NOs: 4-7 (see BQE33274-BQE33277). The
CC invention further discloses: (1) a pharmaceutical composition for
CC preventing or treating a nervous system disease comprising the peptide;
CC (2) a food composition and a health functional food composition for
CC preventing or improving the nervous system disease; (3) a method for
CC preventing or treating a neurological disease; and (4) the use of the
CC peptide in the manufacture of a medicament for preventing or treating the
CC nervous system disease. The peptides of the present invention are useful
CC for preventing or treating nervous system diseases such as multiple
CC sclerosis, neuromyelitis optica, and acute disseminated
CC encephalomyelitis. Parkinson's disease, Alzheimer's disease, amyotrophic
CC lateral sclerosis, Huntington's disease, Menkes disease, Wilson's
CC disease, prion disease, occipital horn syndrome, congenital iron
CC metabolism disorder (Aceruloplasminemia), paresthesia, movement disorder,
CC and optic neuritis. The present sequence represents an Octopus minor
CC ceruloplasmin multicopper oxidase 1 domain peptide mutant (C2H)
CC Om_CP002s1. Note: The present sequence is derived from a parent sequence
CC (see BQE33273).
XX
SQ Sequence 12 AA;
Query Match 47.6%; Score 10; Length 12;
Best Local Similarity 100.0%;
Matches 10; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 8 HVDDHIIGGM 17
||||||||||
Db 3 HVDDHIIGGM 12
SEQ ID NO:7
BQE33277
(NOTE: this sequence has 2 duplicates in the database searched)
ID BQE33277 standard; peptide; 9 AA.
XX
AC BQE33277;
XX
DT 12-DEC-2024 (first entry)
XX
DE O. minor ceruloplasmin multicopper oxidase 1 domain mutant peptide SEQ:7.
XX
KW CP protein; Ceruloplasmin; alzheimers disease; encephalomyelitis; food;
KW huntingtons chorea; iron metabolism disorder; motor neurone disease;
KW movement disorder; multiple sclerosis; mutein; neurological disease;
KW neuromyelitis optica; neuroprotective; optic neuritis; paresthesia;
KW parkinsons disease; prion infection; prophylactic to disease;
KW protein therapy; therapeutic; wilson disease.
XX
OS Callistoctopus minor.
OS Synthetic.
XX
FH Key Location/Qualifiers
FT Misc-difference 2
FT /note= "Wild-type Cys substituted by His"
FT Modified-site 9
FT /note= "C-terminal amide"
XX
CC PN WO2024225597-A1.
XX
CC PD 31-OCT-2024.
XX
CC PF 05-MAR-2024; 2024WO-KR002774.
XX
PR 27-APR-2023; 2023KR-00055716.
XX
CC PA (KOAD ) NAT MARINE BIODIVERSITY INST KOREA.
XX
CC PI Jung SH, Lee JH, Jo SM, Kim HB, An HS;
XX
DR WPI; 2024-B52848/091.
XX
CC PT New peptide comprising specific amino acid sequences used in preparing
CC PT medicine or health functional food composition for preventing, improving
CC PT or treating nervous system disease including multiple sclerosis,
CC PT Parkinsons disease, Alzheimers disease, Menkes disease and/or Wilsons
CC PT disease.
XX
CC PS Claim 1; SEQ ID NO 7; 41pp; Korean.
XX
CC The present invention relates to novel peptides derived from
CC ceruloplasmin shown as SEQ ID NOs: 4-7 (see BQE33274-BQE33277). The
CC invention further discloses: (1) a pharmaceutical composition for
CC preventing or treating a nervous system disease comprising the peptide;
CC (2) a food composition and a health functional food composition for
CC preventing or improving the nervous system disease; (3) a method for
CC preventing or treating a neurological disease; and (4) the use of the
CC peptide in the manufacture of a medicament for preventing or treating the
CC nervous system disease. The peptides of the present invention are useful
CC for preventing or treating nervous system diseases such as multiple
CC sclerosis, neuromyelitis optica, and acute disseminated
CC encephalomyelitis. Parkinson's disease, Alzheimer's disease, amyotrophic
CC lateral sclerosis, Huntington's disease, Menkes disease, Wilson's
CC disease, prion disease, occipital horn syndrome, congenital iron
CC metabolism disorder (Aceruloplasminemia), paresthesia, movement disorder,
CC and optic neuritis. The present sequence represents an Octopus minor
CC ceruloplasmin multicopper oxidase 1 domain peptide mutant
CC (C2H/10_12delGGM) Om_CP002s4. Note: The present sequence is derived from
CC a parent sequence (see BQE33273).
XX
SQ Sequence 9 AA;
Query Match 33.3%; Score 7; Length 9;
Best Local Similarity 100.0%;
Matches 7; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 8 HVDDHII 14
|||||||
Db 3 HVDDHII 9
Kataoka et al. (JP2010183857, published Aug 26, 2010, priority Feb 10, 2009) teach human ceruloplasmin peptide #2 comprising the sequence of -HCHVTDHIHAGM-, which meets the limitation “a peptide represented by an amino acid sequence shown in SEQ ID NO:7”(see the sequence alignment below).
SEQ ID NO:7
AYH38485
ID AYH38485 standard; peptide; 16 AA.
XX
AC AYH38485;
XX
DT 14-OCT-2010 (first entry)
XX
DE Human ceruloplasmin (hCp) peptide #2.
XX
KW biosensor; ceruloplasmin; enzyme electrode; protein detection.
XX
OS Homo sapiens.
XX
CC PN JP2010183857-A.
XX
CC PD 26-AUG-2010.
XX
CC PF 10-FEB-2009; 2009JP-00028988.
XX
PR 10-FEB-2009; 2009JP-00028988.
XX
CC PA (UYKA-) UNIV KANAZAWA.
XX
CC PI Kataoka K, Jp, Sakurai T, Jp, Maeda Y, Jp, Ito T, Jp;
XX
DR WPI; 2010-K58147/59.
XX
CC PT Electrode catalyst used in fuel cell, has multi copper oxidase having
CC PT type I copper, proline residue existing between specific amino acid
CC PT residues, and hydrogen bond between amide proton of residues and sulfur
CC PT atom of cysteine residue.
XX
CC PS Disclosure; Fig 1; 45pp; Japanese.
XX
CC The present invention relates to a novel electrode catalyst which
CC comprises multi copper oxidase. The electrode catalyst comprises multi
CC copper oxidase which contains multiple copper atoms including at least
CC type I copper, proline residue existing between cysteine residue and
CC histidine residue that forms ligand loop among 2 histidine residues, and
CC hydrogen bonds between the amide proton of substituted amino acid
CC residues and sulfur atom of type I copper coordination cysteine residue.
CC The electrode catalyst of the invention is useful in fuel cell as an
CC oxidizing agent and in biosensor for detecting changes in protein and
CC enzyme structure. The present sequence represents a human ceruloplasmin
CC (hCp) peptide which is the main component of an electrode catalyst for
CC use in detecting changes in protein and enzyme structure.
XX
SQ Sequence 16 AA;
Query Match 73.0%; Score 54; Length 16;
Best Local Similarity 75.0%;
Matches 9; Conservative 0; Mismatches 3; Indels 0; Gaps 0;
Qy 1 HCHVDDHIIGGM 12
|||| ||| ||
Db 3 HCHVTDHIHAGM 14
Weimer et al. (EP1598367, published Nov 23, 2005, priority May 18, 2004) teach human ceruloplasmin protein A3 inner subdomain comprising aa 893-1040 of human ceruloplasmin, which comprises “a peptide represented by an amino acid sequence shown in SEQ ID NO:7”(see the sequence alignment below).
SEQ ID NO:7
AEE18673
ID AEE18673 standard; protein; 148 AA.
XX
AC AEE18673;
XX
DT 26-JAN-2006 (first entry)
XX
DE Human ceruloplasmin protein A3 inner subdomain (aa: 893-1040).
XX
KW protein production; protein engineering; gene therapy; blood-clotting;
KW blood clotting disorder; anticoagulant; thrombolytic; hemostatic;
KW hematological disease; factor VIII deficiency; genetic disorder;
KW ceruloplasmin.
XX
OS Homo sapiens.
XX
FH Key Location/Qualifiers
FT Binding-site 83
FT /note= "Metal (T1-Cu61) binding site"
FT Binding-site 129
FT /note= "Metal (T1-Cu61) binding site"
FT Binding-site 134
FT /note= "Metal (T1-Cu61) binding site"
FT Binding-site 139
FT /note= "Metal (T1-Cu61) binding site"
XX
CC PN EP1598367-A1.
XX
CC PD 23-NOV-2005.
XX
CC PF 18-MAY-2004; 2004EP-00011736.
XX
PR 18-MAY-2004; 2004EP-00011736.
XX
CC PA (ZLBB-) ZLB BEHRING GMBH.
XX
CC PI Weimer T, Schulte S, Hofmann K, Hauser H;
XX
DR WPI; 2005-772265/79.
XX
CC PT Producing a modified homolog of human ceruloplasmin for treating or
CC PT preventing hemophilia A comprises adding to a homolog of human
CC PT ceruloplasmin at least one metal binding site that corresponds to a metal
CC PT binding site in human ceruloplasmin.
XX
CC PS Disclosure; Fig 3; 74pp; English.
XX
CC The invention relates to modified nucleic acid sequences coding for
CC coagulation factors, in particular human factor V and human factor VIII
CC and their derivatives. Modified Factor V and factor VIII have enhanced
CC stability and serve as modified homologs of human ceruloplasmin. The
CC invention also relates to a method of producing a modified homolog of
CC human ceruloplasmin. The method involves adding to a homolog of human
CC ceruloplasmin at least one metal binding site that corresponds to a metal
CC binding site or to an incomplete metal binding site in human
CC ceruloplasmin. Modified homologs of human ceruloplasmin, polynucleotides,
CC plasmids or vectors or host cells are useful in the manufacture of a
CC medicament for treating or preventing blood coagulation disorder
CC preferably hemophilia A. The invention also covers a transfer vector for
CC use in gene therapy, which comprises modified DNA sequences of the
CC invention. The present sequence is the human ceruloplasmin protein A3
CC inner subdomain.
XX
SQ Sequence 148 AA;
Query Match 66.7%; Score 82; Length 148;
Best Local Similarity 66.7%;
Matches 14; Conservative 0; Mismatches 7; Indels 0; Gaps 0;
Qy 1 GKWLLHCHVDDHIIGGMSAIY 21
| ||||||| ||| || |
Db 123 GIWLLHCHVTDHIHAGMETTY 143
11. This application contains claims 15-17 drawn to an invention nonelected with traverse in the reply filed on 09/17/2025. A complete reply to the final rejection must include cancellation of nonelected claims or other appropriate action (37 CFR 1.144) See MPEP § 821.01.
12. THIS ACTION IS MADE FINAL. Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
13. Any inquiry concerning this communication or earlier communications from the examiner should be directed to CHANG-YU WANG whose telephone number is (571)272-4521. The examiner can normally be reached Monday-Thursday, 7:00am-5:00pm EST.
Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Jeffrey Stucker can be reached at 571-272-0911. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
Chang-Yu Wang
October 14, 2026
/CHANG-YU WANG/Primary Examiner, Art Unit 1675
Prosecution Insights