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.
Status of Claims
Claims 18, 21, 29, 56-57 and 59-73 are pending and under examination. Claims 1-17, 19-21, 22-28, 30-55 and 58 are canceled.
Maintained Rejections
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.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
Claims 18, 21, 29, 56-57 and 59-73 are rejected under 35 U.S.C. 103 as being unpatentable over Walter et al. (US2016/0046988A1, published 02/18/2016, IDS submitted on 10/06/2023) in view of Blanco et al. (“Analysis of Complex Single-Molecular FRET Time Trajectories”, Methods in Enzymology, vol. 472, 2010, pages 153-178).
With respect to claims 18 and 56, Walter teaches a biosensor (see Fig. 1A). Walter teaches that the capture probe (a nucleic acid capture probe) comprises a biotin moiety (see para. [0012]). Walter teaches a detectably labeled query probe (see para. [0013] and Fig.1A). Walter teaches the association of the query probe with the query region of the nucleic acid to form a hybrid and or the kinetic rate constant K describing the dissociation of the hybrid (see para. [0008]). Walter teaches the capture probe is labeled such as a fluorescent moiety (see bottom of para. [0081]). Walter teaches the kinetics rate constant Kon describing the association of the query probe with the query region of the nucleic acid to form a hybrid and/or the kinetic rate constant Koff describing the dissociation of the hybrid is/are greater than 0.1 min-1 (e.g., greater that approximately 0.002 s-1) (see para. [0102]). Walter teaches labels may be fluorescent dyes alone or in combination with moieties that can suppress or shift emission spectra by fluorescence resonance energy transfer (FRET) (see para. [0077]). Walter teaches vbFRET to calculate an idealized (noise-free) two-state intensity trace that identifies transitions between high and low intensity (e.g., binding and dissociation events) for each candidate (see para. [0182]). Walter also teaches vbFRET to identify both the number of binding events and dwell times in the bound state and unbound state for each candidate molecule (see para. [0232]). Walter teaches the Cy3 and Cy5 for fluorescent probes (see Table 2-continued; Figs. 5; and for example, para. [0257]). Walter teaches in Fig. 1A-B the query probe is attached/hybridized to the target nucleic acid at different positions and Fig. 1B further teaches the specific sequence structure of the capture probe and query probe being attached to a target nucleic acid sequence. Also, Fig. 1B of Walter shows the structure of a query probe moiety and Fig. 5A-D show the time-varying fluorescence signal indicating a plurality of transient associations and dissociations of the query probe moiety with the analyte, which appears to read on the structure of the biosensor comprising a capture probe moiety stably connected to a query probe moiety (e.g., two nucleic acids for capture probe and two nucleic acids for query probe). Note that the terms capture and query probes have not been defined in the specification.
Even though Walter teaches using FRET with capture probe and query probe to identify transitions of association and dissociation events, the reference does not explicitly teach the biosensor is a preassembled construct comprising said capture probe moiety and said query probe moiety and two labels.
Blanco teaches single-molecule methods have given researchers the ability to investigate the structural dynamics of biomolecules at unprecedented resolution and sensitivity (see abstract). Blanco teaches the nature of the transition dipole interaction between the two fluorophores, energy transfer is more efficient when they are in close proximity than when they are further apart (see pg. 154, para. 1 of Introduction). Fig. 9. 1 shows capturing the conformational dynamics of single pre-mRNA molecules through smFRET in time (see pg. 155 and caption). Fig. 9.1 also shows labels of a donor (Cy3) and acceptor (Cy5) fluorophores can be captured simultaneously and recording a time-varying fluorescence signal. Blanco teaches the most common fluorophores used for smFRET are Cy3 (donor) and Cy5 (acceptor) because of their relative brightness and photostability (see pg. 155, para. 1). Blanco further teaches advances in microscopy and sample preparation have allowed FRET to be performed at the single-molecule level with relative ease and reliability and in a commonplace single-molecule FRET (smFRET) experiment, the emissions of the fluorophores attached to an immobilized biomolecule are monitored by wide-field video fluorescence microscopy in real-time (see pg. 155, para. 1).
It would have been obvious to a person of ordinary skill in the art before the effective filing date of the claimed invention to have connected the capture and query probes as taught by Walter as a single biosensor for fluorescence resonance energy transfer (FRET) measurements as taught by Blanco because Walter teaches that labels may be used as fluorescent dyes alone or in combination with moieties that can suppress or shift emission spectra by fluorescence resonance energy transfer (FRET) and Blanco teaches FRET performed at the single-molecule level is easy, reliable to monitor in real-time and provides resolution and sensitivity in detecting nucleic acids’ association and dissociation behaviors. Thus, the person would have labeled the capture probe for FRET detection and connected with the labeled query probe because Walter already teaches using vbFRET software to identify transitions between association and dissociation events and recognizes that the capture probe may be labeled with a fluorescent moiety. Because the capture probe and query probe independently bind to different regions of a target molecule and Blanco teaches the single-molecule FRET containing labels performed at an unprecedented resolution and sensitivity, it would have been obvious to the person to have connected the capture probe and query probe into a single biosensor for fluorescence detection.
Furthermore, it would have been obvious to the person to have additionally labeled the query probe with two labels as a single molecule FRET as taught by Blanco because Walter teaches Cy3 and Cy5 are used as fluorescent probes for detection and query probe attached to the target molecules at different positions (see Figs. 1A-B) and Blanco teaches Cy3 (donor) and Cy5 (acceptor) are recognized in the art for brightness and photostability.
The person would reasonably expected success in adding a label to the capture probe or the query probe for FRET measurements because it has been well understood by Walter and Blanco to measure FRET to through time for identifying transition events. Additionally, the person would have reasonably expected success in combining the capture and query probes of Walter into a longer sequence because Walter recognizes the capture probe and query probe independently bind to different regions of a target molecule.
With respect to claim 21, Walter teaches fluorescence intensity at the emission wavelength of the query probe are recorded as a function of time and a number of transitions greater than 10 recorded during the acquisition time indicates the presence of a target nucleic acid at the discrete location on the solid support (see para. [0138] and Figs. 5).
With respect to claim 29, Figs. 5A-D show wherein recording the time-varying fluorescence signal comprises recording a time-varying wavelength emission intensity or emission intensities within a specific range of wavelengths or multiple ranges of wavelengths.
With respect to claim 56, see above in claim 18.
With respect to claim 57, Walter does not explicitly teach a fluor-quencher pair. Walter does teach Cy3 and Cy5 which read on the structure of labels for fluorophore and quencher. Blanco teaches Cy3 and Cy5 are used as FRET. Therefore, it would have been obvious that the FRET detection used above would have the function of a fluorophore and quencher, as Walter’s labels read on the claimed structure of the claimed label.
With respect to claims 59 and 61, Walter teaches LNA self-structure and melting temperature prediction (see para. [0229]). Walter teaches hybridization properties (e.g., increases thermodynamic stability and melting temperature) of oligonucleotides (see para. [0094]). Walter teaches single target mRNA molecules were hybridized to a high-melting temperature TYE563-labeled locked nucleic acid (LNA) for visualization and immobilization (see pg. 38, para. [0255]).
Although Walter does not explicitly teach melting temperature is within or more than 10oC above the measurement temperature of the assay, it has been settled to be no more than routine experimentation for one of ordinary skill in the art to discover an optimum melting temperature for a result-effective of hybridization in assay detection. "[W]here the general conditions of a claim are disclosed in the prior art, it is not inventive to discover the optimum of workable ranges by routine experimentation" Application of Aller, 220 F.2d 454, 456, 105 USPQ 233, 235-236 (C.C.P.A. 1955). "No invention is involved in discovering optimum ranges of a process by routine experimentation." Id. at 458, 105 USPQ at 236-237. The "discovery of an optimum value of a result effective variable in a known process is ordinarily within the skill of the art.” Absent of unexpected results, it would have been obvious to the person of ordinary skill to discover the optimum melting temperature in an assay for hybridization of a sample because the person would have recognized the complex have a higher melting point to contain integrity during detection and Walter teaches single target mRNA molecules were hybridized to a high-melting temperature TYE563-labeled locked nucleic acid (LNA) for visualization.
With respect to claims 60 and 62, Walter teaches the same structures of a capture probe moiety, target analyte and the query probe moiety (transiently binding to the target analyte) (see above). Therefore, the complexes would have the same average lifetimes because the binding occurs within these three binding elements. Noted that the claims are reciting in a wherein clause and the specification discloses nucleic acids for complexes which read on Walter’s nucleic acid complex.
With respect to claim 63, Walter teaches covalently or noncovalently attachments (see para. [0078]). Walter further teaches covalent modification is PEG (see para. [0144]). Walter also teaches spacer (see para. [0230]). Walter teaches query probe moiety (see Fig. 1B), which are made of covalently linked nucleic acid residues.
With respect to claim 64, Walter teaches two or more query probes comprising different sequences (see para. [0193]). Walter teaches the query probe moiety (see Figs 1A-B and 5A-D), which would have a decoy as the query probe transiently binds to said analyte.
With respect to claim 65, Walter teaches the query probe moiety (see Figs 1A-B and 5A-D), which would have a decoy as the query probe transiently binds to said analyte. Walter teaches hybridization properties (e.g., increases thermodynamic stability and melting temperature) of oligonucleotides (see para. [0094]). Walter teaches single target mRNA molecules were hybridized to a high-melting temperature (see pg. 38, para. [0255]).
Although Walter does not explicitly teach melting temperature is within 10oC above the measurement temperature of the assay, it has been settled to be no more than routine experimentation for one of ordinary skill in the art to discover an optimum melting temperature for a result-effective of hybridization in assay detection. "[W]here the general conditions of a claim are disclosed in the prior art, it is not inventive to discover the optimum of workable ranges by routine experimentation" Application of Aller, 220 F.2d 454, 456, 105 USPQ 233, 235-236 (C.C.P.A. 1955). "No invention is involved in discovering optimum ranges of a process by routine experimentation." Id. at 458, 105 USPQ at 236-237. The "discovery of an optimum value of a result effective variable in a known process is ordinarily within the skill of the art.” Absent of unexpected results, it would have been obvious to the person of ordinary skill to discover the optimum melting temperature in an assay for hybridization of a sample because the person would have recognized the complex have a higher melting point to contain integrity during detection and Walter teaches single target mRNA molecules were hybridized to a high-melting temperature TYE563-labeled locked nucleic acid (LNA) for visualization.
With respect to claim 66, Walter teaches two or more query probes comprising different sequences and comprising different detectable (see para. [0193]). Walter teaches the query probe moiety (see Figs 1A-B and 5A-D), which would have a decoy as the query probe transiently binds to said analyte. Therefore, the complexes would have the same average lifetimes because the binding occurs. Noted that the claims are reciting in a wherein clause and the specification discloses nucleic acids for complexes which read on Walter’s nucleic acids.
With respect to claim 67, Walter does not explicitly teach a fluor-quencher pair. Walter does teach Cy3 and Cy5 which read on the structure of labels for fluorophore and quencher. Blanco teaches Cy3 and Cy5 are used as FRET. Therefore, it would have been obvious that the FRET detection used above would have the function of a fluorophore and quencher, as Walter’s labels read on the claimed structure of the claimed label.
With respect to claims 68-69, Walter teaches a locked nucleic acid capture probe (LNA) (see para. [0006]) and biotin which is a small molecule (Fig. 1A).
With respect to claim 70, Walter teaches target nucleic acid (see abstract and Figs 1A-B).
With respect to claim 71, Walter teaches a capture probe may be immobilized by linking directly to the solid support (see para. [0096]).
With respect to claim 72, Walter teaches noncovalent modification (see para. [0149]) and hybridization (non-covalent) to connect capture probe and query probe (see Fig. 1B).
With respect to claim 73 Walter teaches recording the time-varying fluorescence signal at a discrete location on a solid support or detecting the analyte using fluorescence transition data (see Figs. 1A and 5A-D).
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
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Claims 18, 21, 29, 56-57 and 59-73 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-24 of U.S. Patent No. Patent No. 10093967B2 (‘967) (of record 892 dated 09/28/2024) in view of Blanco et al. (“Analysis of Complex Single-Molecular FRET Time Trajectories”, Methods in Enzymology, vol. 472, 2010, pages 153-178) and Walter et al. (US2016/0046988A1, published 02/18/2016, IDS submitted on 10/06/2023).
With respect to instant claims 18, 21, 29, 56-57, 59, 63-64 and 67-73, Patent No. ‘967 recites a method for detecting a target nucleic acid in a sample, the method comprising: a) immobilizing a single target nucleic acid molecule from the sample to a discrete region of a solid support and providing detectably labeled query probes that associate and dissociate with said single target nucleic acid according to a kinetic rate constant k.sub.on or k.sub.off that is greater than 1 min.sup.−1; b) counting a plurality of time-resolved signal intensity transition events detected within the discrete region and identifying the signal intensity transition events as a candidate signal produced by the repeated association and dissociation of said detectably labeled query probes with said immobilized single target nucleic acid molecule when the number of signal intensity transition events detected within the discrete region is greater than a threshold value; and c) detecting the target nucleic acid in the sample when said candidate signal is detected or when a value of a parameter characterizing said time-resolved signal intensity transition events indicates the presence of said single target nucleic acid molecule in said discrete region, wherein said parameter is selected from the group consisting of τ.sub.on, τ.sub.off, mean τ.sub.on, mean τ.sub.off, time-averaged τ.sub.on, time-averaged τ.sub.off, number of transitions, mean number of transitions, distribution of the number of transitions, mean of the distribution of the number of transitions, median of the distribution of the number of transitions, peak of the distribution of the number of transitions, standard deviation of the distribution of the number of transitions, and shape of the distribution of the number of transitions. Claim 2 recites the detectably labeled query probe is a nucleic acid or a fluorescent query probe. Claim 3 recites a capture probe. Claim 7 teaches the target nucleic acid is a ribonucleic acid. Claim 8 recites that the capture probe comprises a nucleic acid. Claim 13 recites the detectably labeled query probe consists of nucleotides. However, the Patent does not recite the biosensor is a preassembled construct comprising the capture probe moiety and query probe moiety and the capture probe moiety comprises a label.
Blanco has been discussed in the above rejection. It would have been obvious to a person of ordinary skill in the art at the time of filing to have connected the capture and query probes as recited in Patent No. ‘967 into a single biosensor with two labels for fluorescence resonance energy transfer (FRET) measurements as taught by Blanco because Blanco teaches FRET performed at the single-molecule level is easy and reliable to monitor in real-time. Thus, the person would have labeled the capture probe for FRET detection and connected with the labeled query probe because Walter already teaches using vbFRET software to identify transitions between association and dissociation events and recognizes that the capture probe may be labeled with a fluorescent moiety. Because the capture probe and query probe independently bind to different regions of a target molecule and Blanco teaches the single-molecule FRET containing labels performed at an unprecedented resolution and sensitivity, it would have been obvious to the person to have connected the capture probe and query probe into a single biosensor for fluorescence detection.
Also, it would have been obvious to the person to have additionally labeled the query probe with two labels as a single molecule FRET as taught by Blanco because Walter teaches Cy3 and Cy5 are used as fluorescent probes for detection and query probe attached to the target molecules at different positions (see Figs. 1A-B) and Blanco teaches Cy3 (donor) and Cy5 (acceptor) are recognized in the art for brightness and photostability.
The person would reasonably expected success in adding a label to the capture probe or additionally to the query probe for FRET measurements because it has been well understood and recited by the Patent, Walter and Blanco to measure fluorescent probes for identifying transition events.
With respect to claims 60-62, and 65-66, the Patent recites the same structures of a capture probe moiety, target analyte and the query probe moiety (transiently binding to the target analyte) (see above). Therefore, the complexes would have the same average lifetimes because the binding occurs within these three binding elements. Noted that the claims are reciting in a wherein clause and the specification discloses nucleic acids for complexes which read on the Patent’s nucleic acids.
Claims 18, 21, 29, 56-57 and 59-73 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-6, 8-17, 20-21 and 23-24 of copending Application No. 17929809 (‘809) in view of Blanco et al. (“Analysis of Complex Single-Molecular FRET Time Trajectories”, Methods in Enzymology, vol. 472, 2010, pages 153-178) and Walter et al. (US2016/0046988A1, published 02/18/2016, IDS submitted on 10/06/2023).
With respect to instant claims 18, 21, 29, 56-57, 59, 63-64 and 67-73, copending Application No. ‘809 recites a method comprising: a) producing a dataset describing a time-resolved signal comprising a series of signal intensity transition events, wherein the time-resolved signal is produced by: i) immobilizing a target analyte to a solid support via a capture probe; ii) contacting the immobilized target analyte with a detectably labeled query probe that repeatedly and transiently associates with the immobilized target analyte; and iii) detecting signal intensity transition events produced by the repeated transient association and dissociation of the detectably labeled query probe with the immobilized target analyte during a defined observation time; and b) classifying the series of signal intensity transition events according to the following: i) a number of signal intensity transition events within an observation time is greater than a threshold number of signal intensity transition events; ii) a median dwell time or a mean dwell time calculated for a number of signal intensity transition events is greater than a threshold dwell time; and/or iii) a median dwell time or a mean dwell time calculated for a number of signal intensity transition events is less than a maximum dwell time. Copending claim 2 recites wherein the number of signal intensity transition events comprises a number of consecutive signal intensity transition events. Copending claim 3 recites wherein the time-resolved signal comprising a series of signal intensity transition events is produced by recording a signal produced by a process of continuous-time stochastic transitions between two or more states each having a different signal intensity. However, the copending Application ‘809 does not recite the biosensor is a preassembled construct comprising the capture probe moiety and query probe moiety and the capture probe moiety comprises a label.
Blanco has been discussed in the above rejection. It would have been obvious to a person of ordinary skill in the art at the time of filing to have connected the capture and query probes as recited in copending Application No. ‘809 into a single biosensor with two labels for fluorescence resonance energy transfer (FRET) measurements as taught by Blanco because Blanco teaches FRET performed at the single-molecule level is easy and reliable to monitor in real-time. Thus, the person would have labeled the capture probe for FRET detection and connected with the labeled query probe because Walter already teaches using vbFRET software to identify transitions between association and dissociation events and recognizes that the capture probe may be labeled with a fluorescent moiety. Because the capture probe and query probe independently bind to different regions of a target molecule and Blanco teaches the single-molecule FRET containing labels performed at an unprecedented resolution and sensitivity, it would have been obvious to the person to have connected the capture probe and query probe into a single biosensor for fluorescence detection.
Also, it would have been obvious to the person to have additionally labeled the query probe with two labels as a single molecule FRET as taught by Blanco because Walter teaches Cy3 and Cy5 are used as fluorescent probes for detection and query probe attached to the target molecules at different positions (see Figs. 1A-B) and Blanco teaches Cy3 (donor) and Cy5 (acceptor) are recognized in the art for brightness and photostability.
The person would reasonably expected success in adding a label to the capture probe or additionally to the query probe for FRET measurements because it has been well understood and recited by the copending Application, Walter and Blanco to measure fluorescent probes for identifying transition events.
With respect to claims 60-62, and 65-66, the copending Application ‘809 recites the same structures of the query probe moiety (transiently binding to the target analyte) (see above). Therefore, the complexes would have the same average lifetimes because the binding occurs within these three binding elements. Noted that the claims are reciting in a wherein clause and the specification discloses nucleic acids for complexes which read on the Patent’s nucleic acids.
This is a provisional nonstatutory double patenting rejection.
Response to Arguments
Applicant's arguments filed 03/25/2026 have been fully considered but they are not persuasive. The rejections above have been modified in view of the amendments.
Applicant argues on page 8 that the phrases capture probe moiety and query probe moiety have been defined in the specification and the capture probe bind with high thermodynamic stability while the query probe binds with moderate to low thermodynamic stability. A single structural element in Walter cannot simultaneously satisfy both definitions. Applicant argues on page 9 that Walter teaches a fundamentally different architecture because, in Walter, the capture probe and query are separated molecules that are not connected to each other. Walter’s capture probe and query probe each independently hybridize to different regions of a target nucleic acid. Applicant argues on page 10 that Blanco does not teach or suggest converting Walter’s independent and separate capture and query probes into the claimed preassembled biosensor construct.
The arguments are not found persuasive for the following reasons. The instant specification only provides examples (e.g.) of capture probe and query probe. Thus, these cited passages in the Remarks are not explicit definitions of what is capture probe or query probe. However, Walter does teach the recited capture probe and query probe (e.g., Walter Fig. 1). Walter also recognizes that in an embodiment the capture probe is also labeled (see above). Thus, the only difference between Walter’s construct of the capture probe and query probe is that they are not connected prior to contacting the analyte. Because the capture probe and query probe independently bind to different regions of a target molecule and Blanco teaches the single-molecule FRET containing labels performed at an unprecedented resolution and sensitivity, it would have been obvious to the person to have connected the capture probe and query probe into a single biosensor for fluorescence detection. There is nothing that hinder the ability to fluorescently detect of the target in Fig. 1A of Walter when these probes are connected as a single biosensor, as they have been designed to bind to different regions of a target.
Applicant further argues on pages 10-11 secondary considerations support nonobviousness through unexpected results. Applicant argues that Example 3 provides 60-fold improvement compared to the query probe in trans.
The arguments are not found persuasive. Applicant has not provided evidence that commensurate in scope with the claimed subject matter. For example, data of Example 3 are from specific chemical structures of a biosensor that includes specific linkers, decoys, and structures of probes. To show unexpected results, the evidence must be (1) commensurate in scope with the claimed subject matter, In re Clemens, 622 F.2d 1019, 1035, 206 USPQ 289, 296 (CCPA 1980), (2) show what was expected, to "properly evaluate whether a … property was unexpected", and (3) compare to the closest prior art. Pfizer v. Apotex, 480 F.3d 1348, 1370-71, 82 USPQ2d 1321, 1338 (Fed. Cir. 2007). Therefore, the generic limitations of a biosensor comprising capture probe and query probe are not commensurate in scope with Example 3 of the specification.
With respect to claims 59, 61, and 65, Applicant argues on page 11 that these are not optimization parameters within a known system; they define the structural and functional architecture of the biosensor itself, which is not disclosed in Walter. With respect to claims 60, 62, and 66, that the inherency argument is not supportable because the claimed average lifetime relationships are specific to the intramolecular biosensor architecture of claim 18.
The arguments are not found persuasive because Walter’s capture probe and query probe are the same structures as the claimed capture probe and query probe. The claims only recite any connection in a preassembled construct of the capture and query probes. That means, the claims only require capture and query probes. Walter teaches the claimed capture probe and query probe, which would have the same functional ability, as the probes are the same. Because the functional data outcome is dependent on the specific chemical structures of any given capture probe and query probe, it is optimizable.
With respect to the nonstatutory double patenting rejection, Applicant argues that the office to hold the rejection in abeyance until claims are deemed allowable or for the reasons stated above the rejections should be withdrawn. The arguments are not found persuasive and maintained for the reasons above.
Conclusion
No claim is allowed.
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). 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.
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/N.P.N/Examiner, Art Unit 1678
/SHAFIQUL HAQ/Primary Examiner, Art Unit 1678
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