DETAILED ACTION
The examiner of your application in the USPTO has changed. To aid in correlating any papers for this application, all further correspondence regarding this application should be directed to Fernando Ivich, Art Unit 1678.
The finality of the last Office action is withdrawn, and new grounds of rejection are set forth below.
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 .
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
Priority
The present application was filed as a proper National Stage (371) entry of PCT Application No. PCT/EP2020/058626, filed 03/26/2020. Acknowledgment is also made of applicant's claim for foreign priority under 35 U.S.C. 119(a)-(d) to Application No. EP19165356.7, filed on 03/26/2019 in Europe.
Claim Objections
Claims 6, 9, 11 and 13 are objected to because of the following informalities:
In claim 6 lines 2-3, “for measuring the amount of a target substance” appears to be a typographical error, namely it is suggested that “for measuring the amount of a target substance” read as “for measuring an amount of a target substance” (annotations added) in order to improve clarity.
In claim 9 line 1, “for measuring the amount of a target substance” appears to be a typographical error, namely it is suggested that “for measuring the amount of a target substance” read as “for measuring an amount of a target substance” (annotations added) in order to improve clarity.
In claim 11 line 1, "The method according to claim 9 wherein calculation" appears to be a typographical error, namely it is suggested that "The method according to claim 9 wherein calculation" read as "The method according to claim 9, wherein the calculation" (annotations added).
In claim 13 line 8, “filaments.” appears to be a typographical error, namely it is suggested that “filaments.” read as “filaments” (removing the period “.”).
Appropriate correction is required.
Claim Rejections - 35 USC § 112
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 6-15 and 17 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. 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 applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention. This is a written description rejection.
Claims 6 and 9 and its dependent claims require a “self-polymerising biopolymer or a nucleating protein” and “a plurality of self-polymerising biopolymer subunits”. Furthermore, claim 7 requires “an agent to prevent spontaneous nucleation or polymerization of the biopolymer subunits”.
The specification does not describe which amino acid residues, nucleic acid residues, or other molecular components are present in the genus of agents encompassed by claims 6-15 and 17. The specification fails to disclose the structures common to all members of the genus and fails to provide sufficient specific examples of agents to be used. In the absence of a known or disclosed correlation between structure and function, claims which encompass variants defined by their function are generally not considered described. Applicant is directed to MPEP § 2163 for guidelines on compliance with the written description requirement.
Vas-Cath Inc. v. Mahurkar, 19 USPQ2d 1111 (Fed. Cir. 1991), clearly states that “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).
The specification only discloses two example of a self-polymerising biopolymer/subunits, namely actin or tubulin (para. 16, “One example of such a self-polymerising biopolymer is tubulin and, in one embodiment, the actin of the first embodiment is replaced with tubulin” para. 108). The specification discloses only four examples of a nucleating protein, “VopF, VopL, an Arp2/3 complex, or formin” (para. 14). Furthermore, the specification only discloses two examples of an agent that prevents spontaneous nucleation or polymerization of the biopolymer subunits, namely profilin and Tβ4 (para. 72). However, only two examples of a self-polymerising biopolymer/subunits is not considered enough written description support for the broad genus of self-polymerising biopolymers and subunits thereof encompassed by the claims. In the same way, only four nucleating proteins are not enough written description support for the broad genus of nucleating proteins encompassed by the claims. Finally, only two examples of agents that prevent spontaneous nucleation or polymerization of the biopolymer subunits is not enough written description support for the broad genus of agents encompassed by the claims.
The skilled artisan cannot envision the detailed chemical structure of each genus of claimed agents, i.e. a self-polymerising biopolymer or a nucleating protein, a plurality of self-polymerising biopolymer subunits and an agent that prevents spontaneous nucleation or polymerization of the biopolymer subunits. Conception is not achieved until reduction to practice has occurred, regardless of the complexity or simplicity of the method of identification. Therefore, the instant claims do not meet the written description provision of 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph.
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claims 9-15 and 17 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Claim 9 recites “A method for measuring the amount of a target substance, the method comprising: a. providing a plurality of conjugates for measuring the amount of the target substance, wherein each conjugate comprises: i. a binding element capable of binding to the target substance: and ii. a self-polymerising biopolymer or a nucleating protein: b. binding the conjugates to the target substance; c. isolating bound conjugates; d. polymerising biopolymer filaments by a plurality of self-polymerising biopolymer subunits of the self-polymerising biopolymer of the conjugate; e. calculating an amount of the target substance”.
To begin, it is not clear how the conjugate comprising the self-polymerising biopolymer is used in the method for measuring the amount of target substance given that the self-polymerising biopolymer would self-polymerize, thereby affecting the sequence of steps (step d appearing to be effectively incorporated into step a). Indeed, the specification admits that “self-polymerising biopolymers may spontaneously begin polymerising before this is intended. Agents such as thymosin beta 4 (Tβ4) prevent spontaneous nucleation of G-actin, thereby preventing monomeric G-actin from spontaneously polymerising” (para. 20). Therefore, a person having ordinary skill in the art would not recognize the metes and bounds of the claim.
Furthermore, step d is unclear. It is not clear what is meant by “polymerising biopolymer filaments” because this can be interpreted as further polymerising biopolymer filaments (a biopolymer filament being already a polymerised biopolymer) or polymerising biopolymers thereby generating filaments. Given these two possible interpretations, the claim is indefinite. Also, it is not clear what is meant by polymerising “by a plurality of self-polymerising biopolymer subunits of the self-polymerising biopolymer of the conjugate”. This limitation can also be interpreted in multiple ways. For example, given that the biopolymers can spontaneously fragment (para. 78), and spontaneously polymerize (para. 20), this limitation can be referring to the biopolymer subunits being fragmented and polymerized by itself. Furthermore, this limitation can also be interpreted as external subunits causing the polymerization step. However, it is noted that the claim fails to recite a step of adding said subunits, which is unclear. Indeed, the specification discloses that “[t]he plurality of self-polymerising biopolymer subunits once mixed with the conjugate may then begin polymerising from the conjugate” (para. 19). For these reasons, a person having ordinary skill in the art would not be capable of recognizing the metes and bounds of the claim.
Next, it is not clear how step e is performed, i.e. how the amount of target substance is calculated. Indeed, steps a-d are drawn to providing conjugates, binding conjugates to the target, isolating the bound conjugates and polymerizing biopolymer filaments, thus it is unclear how the calculation step e can be performed after steps a-d. In other words, there appears to be a disconnect between steps a-d and step e. The specification paragraph 28 discloses that the “calculation in step e comprises using the calculated number of bound conjugates to calculate the amount of the target substance” (also recited in claim 11). The specification also discloses in paragraph 32 that “a concentration of the bound conjugates is calculated using the following equation:
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” (also recited in claim 13). Furthermore, the specification discloses that “[f]rom this concentration of bound conjugates, the concentration of the target substance can be determined based either on experimentation using known concentrations of the target substance or by calculating a predicted value for the number of conjugate binding sites on the target substance” (para. 33). Therefore, the specification admits that calculating the amount of target substance requires prior knowledge of the amount of target substance or knowledge of the number of conjugate binding sites on the target substance (see also para. 83), none of which are recited in claim 9 or any dependent claims , e.g. 11 and 13, which is unclear.
Note also that the specification fails to clarify how the nucleating protein is used to calculate the amount of target substance. Notably step d and the equation to calculate the concentration of bound conjugate (see claim 13 and specification para. 32) only includes terms related to the biopolymer, not the nucleating protein. Therefore, it is not clear how one can calculate the amount of target substance using the nucleating protein, which is encompassed by the claims.
Furthermore, the specification discloses that after step b, there is spontaneous fragmentation of the polymerized biopolymer filaments (“Once both the conjugate 1 and the free filament 8 have polymerised to a sufficient length, they undergo further spontaneous fragmentation” para. 76) which “complicates the determination of rate of change of rate of polymerization as the time for a given filament to fragment is quite uncertain” (para. 78). Given that the rate of polymerization is used to calculate the amount of target substance (see spec. para. 32 and claim 13), it is not clear how the claimed method would be enabled without addressing the spontaneous fragmentation of the polymer filaments. The specification discloses that “the rate at which filaments undergo fragmentation is made more definite and also increased through the use of sonication” (para. 79). Given that the sonication step is not recited in the claim, the claim is indefinite. Note that claim 12 recites “wherein step d further comprises increasing the rate at which biopolymer filaments undergo fragmentation”, which fails to clearly limit the claim to a sonication step. As disclosed in the specification, “the rate at which filaments undergo fragmentation is made more definite and also increased through the use of sonication” (para. 79), which suggests that a sonication step is required to define the step and thus the claims. Therefore, claim 9 is indefinite and claim 12 fails to define the claim.
For these reasons, a person having ordinary skill in the art would not be capable of recognizing the scope of the claim.
Claims 10-15 and 17 are included in this rejection because they depend from rejected claim 9 but fail to clarify the scope of patent protection sought.
Claim 11 recites the limitation "the calculated number or concentration of bound conjugates" in line 2. There is insufficient antecedent basis for this limitation in the claim. It is not clear what is meant by the calculated number or concentration of bound conjugates because a step of calculating the number or concentration of bound conjugates is not recited in claims 9 or 11. A person having ordinary skill in the art would not be capable of recognizing the metes and bounds of the claim.
Claim 13 recites “wherein a number or concentration of bound conjugates is calculated using the following equation:
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where y|0| is the concentration of bound conjugates at time zero, where A is the total concentration of biopolymer minus the critical concentration of biopolymer, where k is the sum of rate constants of biopolymer subunit addition to filament ends, where m is the average length of the biopolymer filaments and where tl/2 is the time taken to reach the biopolymer concentration that is half of the biopolymer concentration found at steady state”.
However, “where m is the average length of the biopolymer filaments” is not clear. Specifically it is not clear how one determines the average length of the biopolymer filaments. The specification only discloses that “m is the average number of actin monomer-subunits per filament, measured as an average length of filament” (para. 87), but fails to clarify how the length is actually measured. Note that there is spontaneous fragmentation (para. 76) as well as “spontaneous nucleation” (para. 68), which affects the average length of the filaments (“Since the fragmentation does not occur at a fixed length, this complicates the determination of rate of change of rate of polymerisation as the time for a given filament to fragment is quite uncertain” para. 78, “Throughout the reaction, provided that spontaneous nucleation of the actin is minimised, the change in rate of polymerisation varies in a specific manner” para. 85). Because of this, there is a question regarding the metes and bounds of the claim.
Claims 14-15 recite the limitation "the polymerisation state of the biopolymer" in lines 1-2. There is insufficient antecedent basis for this limitation in the claim. It is not clear to what polymerisation state the claim is referring because a step of measuring the polymerisation state of the biopolymer is not recited in claims 9-10. A person having ordinary skill in the art would not be capable of recognizing the metes and bounds of the claim.
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.
Claims 6-12, 14-15 and 17 are rejected under 35 U.S.C. 103 as being unpatentable over Mansson et al. (EP 2092343 B1)-Cited on IDS 9/7/2021 ("Mansson") in view of Tomasevic (US 2006/0003399 A1) (“Tomasevic”).
Regarding claims 6-8, Mansson teaches a “detection conjugate” (Title) for measuring the amount of a target substance (“compound/analyte to be detected as well as a possibility to detect different analytes” para. 6). Mansson teaches a kit (“A fourth aspect relates to a kit comprising several of said detection conjugates” para. 8) comprising: a. a conjugate for measuring the amount of a target substance (paras. 6 and 8) comprising: i. a binding element capable of binding to the substance: and ii. a self-polymerising biopolymer or a nucleating protein (“antibodies are immobilized to filamentous binding fragment(s) which might be cytoskeletal filaments such as actin filaments or micro-tubules…binding fragments such as actin filaments and microtubules can bind recognition elements, such as antibodies and nucleic acid oligomers and at the same time bind reporter molecules (e.g. fluorophores) forming one or more detection conjugate(s)” para. 6). Mansson further teaches that “With a growing elderly population there is also a need of developing early detection methods which at an early stage can detect a disease or disorder, such as cancer or Alzheimer's disease for prevention or individualized and effective treatment” (para. 2).
Mansson fails to teach b. a plurality of self-polymerising biopolymer subunits of the self-polymerising biopolymer of the conjugate, wherein the biopolymer subunits comprises labelled self-polymerising biopolymer subunits, and further comprising an agent to prevent spontaneous nucleation or polymerisation of the biopolymer subunits.
Tomasevic teaches “high-throughput actin polymerization assay” (Title). Tomasevic further teaches a kit comprising a self-polymerising biopolymer or a nucleating protein and b. a plurality of self-polymerising biopolymer subunits of the self-polymerising biopolymer, wherein the biopolymer subunits comprises labelled self-polymerising biopolymer subunits, and further comprising an agent to prevent spontaneous nucleation or polymerisation of the biopolymer subunits (“Some kits for assaying for actin polymerization, for instance, include one, some or typically all of the following: purified actin; acrylodan-labeled-G-actin or pyrene-labeled G-actin, a purified actin nucleator such as those described herein; a purified NPF protein such as those described herein; and a purified upstream regulator such as those described herein” para. 169, “Various proteins bind actin and have various roles (e.g., Stabilizers) such proteins can also be included in the assays to identify agents that modulate their activity and/or to study their interactions with actin. Examples of such proteins include, but are not limited to those listed in Tables 2 and 3” para. 110, see Table 2 “Cofilin…Profilin…Gelsolin…”). Tomasevic further suggests that the kit enables the identification of “agents that can be utilized to modulate a number of cellular activities…agents in the treatment of metastasis of tumors and/or in the treatment of inflammatory diseases” (para. 53). Tomasevic further teaches how to prepare or where to purchase the labeled plurality of self-polymerising biopolymer subunits (“Acrylodan-labeled-G-actin can be prepared as described, for example, by Marriott et al. (Biochemistry 27:6214-6220,1988). Some assays utilize pyrene-labeled-G-actin and monitor its incorporation into F-actin. Pyrene-labeled G-actin can prepared as described, for example, by Kouyama and Mihashi (Eur. J. Biochem. 114:33-38, 1981) and Cooper et al. (J. Muscle Res. Cell Motil. 4:253-262, 1983). It can also be purchased from Cytoskeleton, Inc.” para. 62).
It would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have modified the teachings of Mansson to include b. a plurality of self-polymerising biopolymer subunits of the self-polymerising biopolymer of the conjugate, wherein the biopolymer subunits comprises labelled self-polymerising biopolymer subunits, and further comprising an agent to prevent spontaneous nucleation or polymerisation of the biopolymer subunits taught by Tomasevic because Tomasevic suggests that this enables actin polymerization assays for the identification of agents useful in the treatment of metastasis of tumors and/or in the treatment of inflammatory diseases and Mansson is interested in cancer treatment and prevention, a growing need in the field. A person having ordinary skill in the art would have had a reasonable expectation of success because both Mansson and Tomasevic teach a kit comprising a self-polymerising biopolymer or a nucleating protein for biological assays. Furthermore, Tomasevic teaches how to prepare and where to purchase the labeled plurality of self-polymerising biopolymer subunits. Tomasevic also teaches several examples of agents that prevent spontaneous nucleation or polymerisation of the biopolymer subunits (see Table 2).
Regarding claims 9-10 and 17, although the claim is indefinite (see 112b rejection above), in the interest of compact prosecution, step d. is interpreted as reciting “polymerising the self-polymerising biopolymer or nucleating protein into filaments by adding a plurality of self-polymerising biopolymer subunits of the self-polymerising biopolymer or nucleating protein of the conjugate”.
Mansson teaches a method for measuring the amount of a target substance (“An in vitro method of detection of one or more analyes” claim 1), the method comprising: a. providing a plurality of conjugates for measuring the amount of the target substance, wherein each conjugate comprises: i. a binding element capable of binding to the target substance: and ii. a self-polymerising biopolymer or a nucleating protein (“e) Providing said detection conjugates in a solution” claim 1, para. 6); b. binding the conjugates to the target substance (“f) Incubating said detection conjugates in a solution with a sample containing one or more analytes” claim 1); c. isolating bound conjugates (“The method according to claim 1 or 2 wherein said detection in step g)…by…pelleting by centrifugation” claim 3). Note that although Mansson fails to use the language “isolating bound conjugates” the teaching of centrifuging the bound conjugates inherently provides a step of isolating the bound conjugates because the centrifugation effectively separates the bound conjugates as a pellet from the rest of the solution. Mansson further teaches e. calculating an amount of the target substance (“h) Optionally analysing the aggregate formed” claim 1, “analysis in step h) is by ocular inspection, microscope, light scattering, pelleting by centrifugation, spectrophotometry, fluorescence detection, surface enhanced Raman scattering or surface plasmon resonance” claim 3). Note that although Mansson fails to use the language “calculating an amount of the target substance” the teaching of “analysing the aggregate formed” by “by ocular inspection, microscope, light scattering…” inherently provides the calculating an amount of the target substance because Mansson teaches that “quantitative information about concentration of analyte may be obtained from the amount of aggregates” (para. 25), which reads on the claim.
Mansson fails to teach d. polymerising the self-polymerising biopolymer or nucleating protein into filaments by adding a plurality of self-polymerising biopolymer subunits of the self-polymerising biopolymer or nucleating protein of the conjugate, d2. measuring a time value indicative of the time taken for polymerisation and depolymerisation of the biopolymer to reach steady state, and d3. using the time value to calculate a number or concentration of the bound conjugates.
Tomasevic teaches “high-throughput actin polymerization assay” (Title). Tomasevic further teaches d. polymerising a self-polymerising biopolymer or nucleating protein into filaments by adding a plurality of self-polymerising biopolymer subunits of the self-polymerising biopolymer or nucleating protein (“(a) combining actin polymerization assay components in the presence of a test agent, the components comprising (i) pyrene-G-actin (pyrene-globular actin) or acrylodan-G-actin (acrylodan-globular actin), (ii) anArp2/3 complex, (iii) a nucleation promoting factor (NPF) protein that can initiate nucleation of actin…and (iv) and an upstream regulator that can activate the NPF protein…” claim 1). Tomasevic further teaches how to prepare or where to purchase the labeled plurality of self-polymerising biopolymer subunits (“Acrylodan-labeled-G-actin can be prepared as described, for example, by Marriott et al. (Biochemistry 27:6214-6220,1988). Some assays utilize pyrene-labeled-G-actin and monitor its incorporation into F-actin. Pyrene-labeled G-actin can prepared as described, for example, by Kouyama and Mihashi (Eur. J. Biochem. 114:33-38, 1981) and Cooper et al. (J. Muscle Res. Cell Motil. 4:253-262, 1983). It can also be purchased from Cytoskeleton, Inc.” para. 62). Tomasevic further teaches d2 measuring a time value indicative of the time taken for polymerisation and depolymerisation of the biopolymer to reach steady state (“(b) detecting fluorescence over time to determine a fluorescence parameter that is a measure of the polymerization of pyrene-G-actin into pyrene-F-actin (pyrene filamentous actin) or acrylodan-G-actin into acrylodan F-actin (acrylodan-filamentous actin)” claim 1, “In general, a signal associated with polymerization is detected over time. Recording signal formation as actin polymerizes typically yields a sigmoidal curve. This is because initially there is a lag phase. This lag phase is typically followed by a relatively rapid increase in signal as the nucleated actin begins to polymerize. Eventually the signal reaches a plateau once most of the G-actin has become incorporated into F-actin” para. 121). Tomasevic further suggests d3. using the time value to calculate a number or concentration of the bound conjugates (“(c) comparing the polymerization parameter determined in (b) with the polymerization parameter for a control reaction conducted in the absence of agent, wherein a difference is an indication that the agent is a modulator of the activity of one of the polymerization components” claim 1, “The total rate of G-actin to F-actin conversion is linearly related to the number of filament ends and to the G-actin concentration” para. 55). Tomasevic further suggests that steps d, d2 and d3 enable the identification of “agents that can be utilized to modulate a number of cellular activities…agents in the treatment of metastasis of tumors and/or in the treatment of inflammatory diseases” (para. 53)
It would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have modified the teachings of Mansson to include steps d, d2 and d3 taught by Tomasevic because Tomasevic suggests that this enables actin polymerization assays for the identification of agents useful in the treatment of metastasis of tumors and/or in the treatment of inflammatory diseases and Mansson is interested in cancer treatment and prevention. A person having ordinary skill in the art would have had a reasonable expectation of success because both Mansson and Tomasevic teach self-polymerising biopolymer or a nucleating protein for biological assays. Furthermore, Tomasevic teaches how to prepare and where to purchase plurality of self-polymerising biopolymer subunits.
Regarding claim 11, Mansson in view of Tomasevic teach the method of claim 9 as discussed above.
Mansson in view of Tomasevic further teach wherein calculation in step e comprises using the calculated number or concentration of bound conjugates to calculate the amount of the target substance (“Quantitative information about concentration of analyte may be obtained from the amount of aggregates” Mansson para. 25).
Regarding claim 12, Mansson in view of Tomasevic teach the method of claim 9 as discussed above.
Mansson in view of Tomasevic further teach wherein step d further comprises increasing the rate at which biopolymer filaments undergo fragmentation (“combining…and (iv) and an upstream regulator that can activate the NPF protein, wherein the upstream regulator is selected from the group consisting of a Cdc42 protein, a Rac1 protein, a Nckl protein, a Nck2 protein and phosphatidylinositol-1,4-bisphosphate (PIP2)” claim 1 of Tomasevic, see Figure 12).
Regarding claims 14-15, although the claim is indefinite (see 112b rejection above), in the interest of compact prosecution, the claims are interpreted as being drawn to step e. Mansson in view of Tomasevic teach the method of claim 10 as discussed above.
Mansson in view of Tomasevic further teach wherein the polymerisation state of the biopolymer is measured by using fluorescently labelled biopolymer, and wherein the polymerisation state of the biopolymer is measured by the level of light scattering caused by the biopolymer filaments (“The method according to claim 1 or 2 wherein…analysis in step h) is by…light scattering…fluorescence detection” claim 3 of Mansson).
Pertinent Prior Art
The prior art made of record and not relied upon is considered pertinent to applicant's disclosure.
Doolittle et al. Methods Mol Biol. 2013 ; 1046: 273–293. doi:10.1007/978-1-62703-538-5_16 (“Doolittle”). Dolittle teaches “how to perform and analyze these in vitro actin polymerization assays, with an emphasis on extracting useful descriptive parameters from kinetic data” (Abstract). Doolittle further teaches “3.3. Analysis of Pyrene Actin Polymerization Assays” (page 10). Doolittle teaches the equation on how to “Find [Actin](t1/2), the remaining free actin at t1/2” (page 12 point 9), namely
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However, Doolittle fails to teach the equation of claim 13. Claim 13 seems to be free of the art. Indeed, Doolittle appears to teach away from a single equation that can be used to calculate the concentration of bound conjugates (“[a]nalysis of the resulting kinetic profiles is somewhat complicated. The difficulty stems from the fact that polymerization kinetics are a combination of processes: elongation of filaments at both their fast growing ‘barbed’ end and their slow growing ‘pointed’ end, nucleation of new filaments from bulk solution, and nucleation of filaments in a filament dependent manner. These processes all have distinct kinetic effects. There is no general analytic solution for actin polymerization kinetics in the presence of nucleation factors, and thus descriptive metrics for the kinetics are typically used for quantification instead of parameters determined by fitting to the entire dataset (see Note 1)” (page 2 para. 3).
Response to Arguments
Applicant’s arguments, see Remarks page 4, filed 5/27/2026, with respect to the alleged allowable subject matter, have been fully considered but are not persuasive.
Applicant argues that “the Examiner explicitly recognized that “Claims 6-15 and 17 are free of prior art””.
However, the current Examiner fails to recognize that all of claims 6-15 and 17 are free of prior art (see 103 rejections above). In fact, the claims are rejected under 112a, 112b and 103 (see rejections above).
Conclusion
No claim is allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to FERNANDO IVICH whose telephone number is (703)756-5386. The examiner can normally be reached M-F 9:30-6:00 (E.T.).
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/Fernando Ivich/Examiner, Art Unit 1678
/GREGORY S EMCH/Supervisory Patent Examiner, Art Unit 1678
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