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and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114.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 09/19/2025 has been entered.
Information Disclosure Statement
The information disclosure statement (IDS) dated 09/19/2025 comply with the provisions of 37 CFR 1.97, 1.98 and MPEP § 609. Accordingly, they have been placed in the application file and the information therein has been considered as to the merits.
Status of the application
Receipt of applicant’s remarks with filed declaration and claim amendments filed on 09/19/2025 are acknowledged.
However, applicants’ arguments and filed declaration are found not persuasive. Accordingly, the previous 112(a) written description rejection is maintained.
In addition, a new 112(a) enablement rejection is made.
Please see the examiners response to applicants below.
Response to Arguments
It appears that applicants filed arguments are nothing but repeating the same arguments in different way, but the main argument is about the shown data in the filed declaration as an evidence for the claimed method. In fact, applicants presented arguments in the filed response are already addressed and clarified concerns in the previous office action(s). Moreover, applicants failed to address examiner’s provided reasoning from the previous office actions, specifically examiner’s response on the shown data in the declaration.
As explained in the rejection, originally filed specification fails to describe or show any evidence of how an amino acid finds its right location in right order or what drives an amino acid to a right place and forms a specific peptide bond in specific order? There is a high level of “unpredictability” in applicant achieving the successful making of duplicate peptides/proteins utilizing the exemplified protocols coupled with a lack of clear objective evidence that demonstrates their success in meeting their claimed synthetic objective.
As explained in the previous response, shown data in the filed declaration, such evidences cannot be used to cure an otherwise defective specification/disclosure, as evidenced from the board cases. See Appeal 2021-002851 (15/993,172) (“In short, Dr. Steinman’s declaration makes clear that the therapeutic data, which is not part of Appellant’s Specification, is part of the data that he considers necessary to provide reasonable predictability of treatment with a blocking antibody to CD49e to enable the claimed invention without undue experimentation … Notably, Dr. Block does not state that he has only reviewed the experimental work set forth in the Specification. See In re Wright, 999 F.2d 1557, 1563 (Fed. Cir. 1993) (noting that declaration evidence failed to support enablement because the declarants did not even indicate in their affidavits that they reviewed the Specification … While a post-filing declaration may be used to show the accuracy of a statement in the specification, it cannot ‘render an insufficient disclosure enabling.’ In re Brana, 51 F.3d 1560, 1567 n.19 (Fed. Cir. 1995).”). See also Appeal 2021-002851 (15/993,172) (“Paragraph 102 of the Specification just generally identifies a broad range of “effective dose of an anti-α5 agent of the invention [that can be] administered alone, or combined with additional active agents for the treatment of a condition as listed above.” There is nothing else in the Specification for one of ordinary skill in the art to determine what dose and agent would be able to treat ALS in humans in the manner required by the claims. As noted, Dr. Steinman’s Declaration refers to an experiment that may shed light on that, but that evidence is not part of the Specification, and it is not even clear that the experiment was carried out by the time of the effective filing date of the application. While a post-filing declaration may be used to show the accuracy of a statement in the specification, it cannot “render an insufficient disclosure enabling.” In re Brana, 51 F.3d 1560, 1567 n.19 (Fed. Cir. 1995).”).
So while a post-filing declaration can be used for some purposes (e.g., show what the state of the art was as of the effective filing date, verify statements in the specification as truthful, etc.), it cannot be used to replace the specification. Remember too that enablement must occur as of the filing date, not some later date. “Enablement, or utility, is determined as of the application filing date.” In re Brana, 51 F.3d 1560, 1567 n.19, 34 USPQ2d 1436, 1441 n.19 (Fed. Cir. 1995). See Appeal 2007-4458 (09/036,613) (“[A]lthough evidence obtained after the application’s filing can be used to verify the accuracy of statements already in the Specification, it cannot be used to supplement the Specification’s disclosure. See id.; see also In re Hogan, 559 F.2d 595, 605, (CCPA 1977) (‘[U]se of later publications as evidence of the state of art EXISTING on the filing date of an application” is acceptable.’”).
This suggests that Applicants did not provide an sufficient description so that a skilled person can understand or enabling disclosure as of the filing date. Later experiments proving these things (even if they existed) would not be enough. Again, the specification must describe and enable the invention, not some later experiments performed by the Applicants. See Appeal 2015-007406 (13/880,113) (“It is an applicant’s obligation to supply enabling disclosure without reliance on what others may publish after he has filed an application on what is supposed to be a completed invention. If he cannot supply enabling information, he is not yet in a position to file.” In re Glass, 492 F.2d 1228, 1232 (CCPA 1974).”). It sounds like maybe Applicants jumped the gun here and filed too quickly (assuming the invention works at all)?
Above reasoning is also applicable to applicants filed declaration on 09/19/2025.
Claim Rejections - 35 USC § 112 – Written Description [Maintained]
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 25, 27-32 and 34-41 are rejected 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 for the claimed product. 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 based on the requirement(s), i.e., the guidelines provided by the MPEP 2163.04. These are listed below:
(A) identify the claim(s) limitations at issue, and
(B) establish a prima facie case by providing reasons why a person skilled in the art at the time the application was filed would not have recognized that the inventor was in possession of the invention as claimed in view of the disclosure of the application as filed. The MPEP 2163 further provided or expanded the guidelines for the written description requirements.
(A) IDENTIFY THE CLAIM LIMITATIONS AT ISSUE:
Independent claim 25 is drawn to a method of synthesizing a peptide, comprising adding (a) a quantity of a template peptide having 10-200 amino acids; and
(b) a mixture of individual amino acids that are not activated, and are capable of forming copies of the template peptide into an aqueous solution; and
(c) providing about 1.2 kcal/mol of energy to the aqueous solution of the template peptide and the mixture of individual amino acids, wherein the energy is sufficient to result in sequence-specific peptide bond formation of individual amino acids from the mixture of individual amino acids based on the template peptide amino acid sequence.
The dependent claims drawn to the reaction conditions, such as temperature, source of energy, optionally buffered solutions, concentrations of individual amino acids and template, and absence of nucleic acids, enzymes or coenzymes etc.
Based on the claim language the claimed process can be interpreted as a method of synthesizing a peptide, ranges from 10-200 amino acids, by mixing a protein of interest and its individual amino acids in pure water or buffered water, by providing about 1.2 kcal/mol of energy, wherein the reaction is maintained at a constant temperature of 10o to 100oC, wherein the energy source is either heating or exposing the aqueous solution to full spectrum light.
The specification describes that the peptides can be synthesized in an aqueous solution such as pure water in the absence of nucleic acids, enzymes or co-enzymes or other cellular material or cells only using a template peptide and amino acids and "a low amount of energy". Figures 1-3 and Table 2 show the amplification of peptides of 4 to 20 amino acids and of insulin (110 amino acids). According to Table 2, the amount of protein produced was 27 to 201% of the amount of the template peptide after an incubation at 40°C and using a constant source of full spectrum light. Figures 4-9 summarize the results of experiments intended to show the lack of contamination by the presence of DNA or RNA, enzymes or living cells. Also, it seems impossible that at temperatures as low as 10°C a peptide bond is created and at temperatures as high as 100°C, is not denaturized.
However, specification fails to describe or show any evidence of how an amino acid finds its right location or right order or what drives an amino acid into a right direction and forms a sequence specific peptide bond? Further, peptides fold correctly if they are in an appropriate environment, however, water is not sufficient for folding process.
In the shown data in the specification, there is no actual mass spectrum is shown for the synthesized peptide, nor a comparative MS spec for synthesized peptide with a template peptide. In other words, individual mass spectra for synthesized peptide and template peptide are not shown, which is one of the critical evidence, to understanding the claimed invention. Simply increase in the mass, as shown in Tables, which is not an art recognized evidence for the formation of peptide bond or peptide self-replication. It can be different peptide with same mass. Moreover, it appears that applicants description in specification is nothing but simple statements and not an actual evidences towards formation of desired peptide using a template.
In absence of such evidences, a skilled person cannot understand applicants claimed invention.
So, the question is with several uncertainties in the claimed subject matter, (i) did applicants provide enough description and evidences for making the claimed peptide synthesis? (ii) will a skilled person in the art understand the claimed invention based on the provided description or examples in the specification?
The MPEP lists factors that can be used to determine if sufficient evidence of possession has been furnished in the disclosure of the application. These include "level of skill and knowledge in the art, partial structure, physical and/or chemical properties, functional characteristics alone or coupled with a known or disclosed correlation between structure and function, and the method of making the claimed invention. Disclosure of any combination of such identifying characteristics that distinguish the claimed invention from other materials and would lead one of skill in the art to the conclusion that the applicant was in possession of the claimed species is sufficient" (MPEP 2163).
(B) ESTABLISH A PRIMA FACIE CASE BY PROVIDING REASONS WHY A PERSON SKILLED IN THE ART AT THE TIME THE APPLICATION WAS FILED WOULD NOT HAVE RECOGNIZED THAT THE INVENTOR WAS IN POSSESSION OF THE INVENTION AS CLAIMED IN VIEW OF THE DISCLOSURE OF THE APPLICATION AS FILED:
The further analysis for adequate written description considers, see MPEP 2163, the following:
(A) Determine whether the application describes an actual reduction to practice of the claimed invention:
Not provided. The whole description appears to be hypothetical and no evidence is shown for the claimed subject matter.
In the Experiment 1, the specification shown the preparative method of linear peptide VR15 by simply adding template peptide and amino acid solution at the recited concentrations and incubated at 37oC with a full spectrum of light for up to 4 hrs. Followed by reverse phase C18 chromatography, and then Mass spectrometer to measure the intensity of heavy (synthesized peptide) and light (template peptide) versions of the peptide, as shown in Fig. 1D.
Similarly, in Experiment 2, the specification described the preparation of insulin, MRFA, VR9 and WK20 using corresponding peptide templates.
The chromatography is useful to separate peptide or its fragments, and it does not tell the amino acid sequence. Mass spec is useful to identify the charged fragments, which can be useful to identify the amino acid sequence. However, there is actual mass spectrograms are shown for template and synthesized peptides. Examples simply say ‘increase in the mass’ is evidence of formation of peptide from its template.
So, the provided data is very limited and not supporting evidence for the claimed subject matter.
Accordingly, applicants failed to describe actual reduction to practice of the claimed invention.
(B) If the application does not describe an actual reduction to practice, determine whether the invention is complete as evidenced by a reduction to drawings or structural chemical formulas that are sufficiently detailed to show that applicant was in possession of the claimed invention as a whole:
Fig.1-3 shows quantitative analysis of template peptide and synthesized peptides and conclude that increase in the mass of peptide indicates the formation of copy of a template peptide. No actual individual mass spectra are shown.
Fig. 4 simply shows absence of biological contamination in the samples.
Fig. 5 shows a test for presence of DNA or RNA in the samples.
It appears that the experiments in Fig. 6-8 are not relevant to the claimed subject matter.
Fig.9 is mass spectra of individual amino acids, not the peptides. Applicants should have shown similar data for the synthesized peptides and template peptides.
Fig.10 is a theoretical description of claimed method.
Fig. 11 shows a chromatogram for the insulin synthesis, but no evidence of actual amino acid sequence for the synthesized peptide is provided.
It appears that Fig. 12-20 are purely or semi theoretical and do not support for the evidence of amino acid sequence of synthesized peptide using template peptide.
So, as explained above, none of the drawings show or describe actual sequence analysis or evidence of sequence of synthesized peptide, and not even template peptide. The invention is also not completely described with shown drawings or structural chemical formulas, which are not sufficiently detailed to show that applicant was in possession of the claimed invention as a whole.
(C) If the application does not describe an actual reduction to practice or reduction to drawings or structural chemical formula as discussed above, determine whether the invention has been set forth in terms of distinguishing identifying characteristics, such as structure/function correlations, as evidenced by other descriptions of the invention that are sufficiently detailed to show that applicant was in possession of the claimed invention:
It appears that the application provides a hypothesis that the synthesis reaction can be explained by organization of amino acids according to "structural compatibility", wherein an amino acid "sits on" the identical amino acid of the template peptide due to its similar structure, i.e. arginine "sits on" arginine in the template and a low energy provided to the system is sufficient to create peptide bonds between amino acids in close proximity.
However, the above hypothesis goes against common general knowledge. It seems impossible that amino acids always interact with identical amino acids of the peptide. In particular, the twenty naturally occurring amino acids comprise the group of negatively charged amino acids and the group of positively charged amino acids. A negatively charged amino acid will not "sit on" a negatively charged amino acid but will be attracted by a positively charged amino acid. Similarly, a positively charged amino acid will not "sit on" a positively charged amino acid but will be attracted by a negatively charged amino acid. Similar considerations apply for the polar amino acids. Finally, although the non-polar amino acids are likely to interact with further non-polar amino acids, one non-polar amino acid does not always interact with the same non-polar amino acid, i.e. alanine does not always "sit on" alanine but may also be attracted e.g. by valine. Hence, it is not credible that a template peptide/protein favors the formation of peptides/proteins of the same sequence.
In other words, it seems impossible that a template peptide determines the order of the amino acids in a different peptide, since there are no known chemical or physical forces of amino acids in a peptide attracting the same amino acid so that said amino acids could be linked in a peptide of the same sequence. Such "pairing" is only known for complementary nucleobases.
In view of above contradictions the claimed subject-matter is not supported by the description, so that a skilled person can understand applicants claimed invention. Without a correlation between structure and function, the claims do little more than define the claimed invention by function. That is not sufficient to satisfy the written description requirement.
Accordingly, it is deemed that the specification fails to provide adequate written description for the claimed subject matter and does not reasonably convey to one skilled in the relevant art that the inventors had possession of the claimed invention.
Claim Rejections - 35 USC § 112(a) Enablement [New]
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 25, 27-32 and 34-41 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the enablement requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to enable one skilled in the art to which it pertains, or with which it is most nearly connected, to make and/or use the invention.
The MPEP 2164.01(a), states that there are many factors to be considered when determining whether there is sufficient evidence to support a determining that a disclosure does not satisfy the enablement requirement and whether any necessary experimentation is “undue”.
Pursuant to In re Wands, 858 F.2d 731, 737, 8 USPQ2d 1400, 1404 (Fed. Cir. 1988), one considers the following factors to determine whether undue experimentation is required: (1) The breadth of the claims; (2) The nature of the invention; (3) The state of the prior art; (4) The level of one of ordinary skill; (5) The level of predictability in the art; (6) The amount of direction provided by the inventor; (7) The existence of working examples; and (8) The quantity of experimentation needed to make or use the invention based on the content of the disclosure.
Criticality of this rejection is the fact that specification fails to describe or show any evidence of how an amino acid finds its right location or right order or what drives an amino acid into a right direction and forms a sequence specific peptide bond? How a negatively charged amino acid will "sit on" a negatively charged amino acid, and in fact it will be attracted by a positively charged amino acid. Similarly, a positively charged amino acid will not "sit on" a negatively charged amino acid. It’s against nature.
The above factors are applied to claims the analysis is as follows:
(1) The breadth of the claims:
Independent claim is drawn to a method of synthesizing a peptide, comprising:(a) providing a template peptide having from about 10 amino acids to about 200 amino acids; (b) providing a mixture of individual amino acids that are not activated, and are capable of forming copies of the template peptide into an aqueous solution, wherein the individual amino acids in the mixture of individual amino acids are in an amount that is at least equal to the stoichiometric amount of each amino acid in the template peptide sequence; (c) contacting the template peptide and the mixture of individual amino acids in an aqueous solution at a reaction temperature of from about 20oC to about 50°C; (d) providing at least about 1.2 kcal/mol of energy in the form of full spectrum light to the aqueous solution of the template peptide and the mixture of individual amino acids, wherein the energy is sufficient to result in sequence-specific peptide bond formation of individual amino acids from the mixture of individual amino acids based on the template peptide amino acid sequence; and (e) performing step (d) for a time period sufficient to synthesize the peptide from the mixture of individual amino acids, wherein the amino acid sequence of the peptide is the same as the amino acid sequence of the template peptide.
The dependent claims drawn to the reaction conditions, such as temperature, source of energy, optionally buffered solutions, concentrations of individual amino acids and template, and absence of nucleic acids, enzymes or coenzymes etc.
Based on the claim language the claimed process can be interpreted as a method of synthesizing a peptide, ranges from 10-200 amino acids, by mixing a protein of interest as a template peptide (to be made) and its individual amino acids in pure water or buffered water, by providing at least about 1.2 kcal/mol of energy, wherein the reaction is maintained at a constant temperature of 20o to 50oC, wherein the energy source is either heating or exposing the aqueous solution to full spectrum light.
(2) The nature of the invention:
It is a peptide synthesis, but it is totally different from the conventional one. Claimed peptide synthesis, which is “templated method”, does not require coupling reagents, use of complex chemistry, high temperature and/or pressure or DNA templates to facilitate peptide synthesis, only the peptide to be synthesized (as a template peptide) and their corresponding constituent amino acids are required.
The presence of the template peptide provides organization of the amino acids by virtue of structural compatibility with like amino acids i.e., it is considered that arginine will 'sit on' an arginine in the template peptide due to the similar structure, likely retarding its movement. Suitably, it is considered that sequence selective molecular recognition on complementary surfaces has a pivotal role in peptide self replication. It is considered this will occur with the other amino acids in the sequence and bring them into close proximity to each other. The system provides energy sufficient enough to enable the peptide bond formation to occur between amino acids and for templated synthesis of the peptide to occur.
Thus, to be enabled for the invention one of ordinary skill in the art must accept that a negatively charged amino acid will "sit on" a negatively charged amino acid, and a positively charged amino acid will "sit on" a positively charged amino acid and, coupling takes between two sitting adjacent amino acids on template peptide without any coupling reagents.
(3) The state of the prior art:
So far as the examiner is aware, the prior art does not appear to provide any evidence of applicants claimed ‘templated method’ for synthesizing peptides by mixing template peptide and its corresponding individual amino acids.
(4) The level of predictability in the art:
It appears that predictability in the art is very low, because claimed peptide synthesis from ‘templated method’ goes against natural attractions and common general knowledge. A positively charged amino acid will not sit on positively charged amino acid, but will get attracted towards negatively charged amino acid.
Known art is limited to classical solid or liquid phase peptide synthesis using protected amino acids with specific conditions and specific reagents.
(5) The level of one of ordinary skill: moderately high based on the level of education and research in the art.
(6) The amount of direction provided by the inventor:
The specification describes that the peptides can be synthesized in an aqueous solution such as pure water in the absence of nucleic acids, enzymes or co-enzymes or other cellular material or cells only using a template peptide and amino acids and "a low amount of energy". Figures 1-3 and Table 2 show the amplification of peptides of 4 to 20 amino acids and of insulin (110 amino acids). According to Table 2, the amount of protein produced was 27 to 201% of the amount of the template peptide after an incubation at 40°C and using a constant source of full spectrum light. Figures 4-9 summarize the results of experiments intended to show the lack of contamination by the presence of DNA or RNA, enzymes or living cells. Also, it seems impossible that at temperatures as low as 10°C a peptide bond is created and at temperatures as high as 100°C, is not denaturized.
However, specification fails to describe or show any evidence of how an amino acid finds its right location or right order or what drives an amino acid into a right direction and forms a sequence specific peptide bond? Further, peptides fold correctly if they are in an appropriate environment, however, water is not sufficient for folding process.
In the shown data in the specification, there is no actual mass spectrum is shown for the synthesized peptide, nor a comparative MS spec for synthesized peptide with a template peptide. In other words, individual mass spectra for synthesized peptide and template peptide are not shown, which is one of the critical evidence, to understanding the claimed invention. Simply increase in the mass, as shown in Tables, which is not an art recognized evidence for the formation of peptide bond or peptide self-replication. It can be different peptide with same mass. Moreover, it appears that applicants description in specification is nothing but simple statements and not an actual evidences towards formation of desired peptide using a template.
In absence of such evidences or guidelines, a skilled person cannot understand applicants claimed invention.
(7) The existence of working examples:
In the Experiment 1, the specification shown the preparative method of linear peptide VR15 by simply adding template peptide and amino acid solution at the recited concentrations and incubated at 37oC with a full spectrum of light for up to 4 hrs. Followed by reverse phase C18 chromatography, and then Mass spectrometer to measure the intensity of heavy (synthesized peptide) and light (template peptide) versions of the peptide, as shown in Fig. 1D.
Similarly, in Experiment 2, the specification described the preparation of insulin, MRFA, VR9 and WK20 using corresponding peptide templates.
The chromatography is useful to separate peptide or its fragments, and it does not tell the amino acid sequence. Mass spec is useful to identify the charged fragments, which can be useful to identify the amino acid sequence. However, there is actual mass spectrograms are shown for template and synthesized peptides. Examples simply say ‘increase in the mass’ is evidence of formation of peptide from its template.
So, the provided data is very limited and not supporting evidence for the claimed subject matter.
(8) The quantity of experimentation needed to make or use the invention based on the content of the disclosure:
The skilled practitioner would first turn to the instant description for guidance in using the claimed invention. However, the description lacks clear experimental evidence for making peptide from its template peptide and corresponding individual amino acids. As such, the skilled practitioner would turn to the prior art for such guidance, however the prior art does not discuss applicants ‘template method’. Finally, said practitioner would turn to trial and error experimentation to determine a relationship between template peptide and its corresponding individual amino acids, by the claimed methodology to make peptide. However, such amounts to undue experimentation.
As such, claims are not enabled.
Conclusion
Any inquiry concerning this communication or earlier communications from the examiner should be directed to SUDHAKAR KATAKAM whose telephone number is (571)272-9929. The examiner can normally be reached 8:30 am to 5 pm.
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, Melissa Fisher can be reached at 571-270-7430. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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SUDHAKAR KATAKAM
Primary Examiner
Art Unit 1658
/SUDHAKAR KATAKAM/Primary Examiner, Art Unit 1658