CTNF 18/285,134 CTNF 95854 DETAILED ACTION Notice of Pre-AIA or AIA Status 07-03-aia AIA 15-10-aia The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA. 07-06 AIA 15-10-15 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. Claim Rejections - 35 USC § 103 07-20-aia AIA 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. 07-23-aia AIA 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. 07-21-aia AIA Claim s 1-5 are rejected under 35 U.S.C. 103 as being unpatentable over “High performance plasma amyloid-β biomarkers for Alzheimer’s disease” to Nakamura et al. (herein Nakamura) as cited on the 04 October 2023 IDS in view of US 2017/0016910 to Kaneko as cited on the 04 October 2023 IDS . Regarding claims 1 and 5 , Nakamura discloses a method for creating standardization curves (i.e., calibration curves) for quantifying Aβ1-40, Aβ1-42, and APP669-711 (i.e., amyloid β-related peptide) (see Extended Data Figure 5 Reliability of the IP-MS methods), the method comprising the steps of: providing a plurality of standard solutions containing the amyloid β-related peptide and PBS containing BSA and having different concentrations of the amyloid β-related peptide ) (see Extended Data Figure 5 Reliability of the IP-MS methods); mixing a solution containing internal standard peptide with each of the plurality of standard solutions to obtain a plurality of calibration curve solutions (see Plasma Aβ measurements and Extended Data Figure 5 Reliability of the IP–MS methods); performing immunoprecipitation and mass spectrometry (IP-MS) on the plurality of calibration curve solutions to obtain signal intensity of the amyloid β-related peptide and the internal standard peptide for each of the plurality of calibration curve solutions (see Plasma Aβ measurements and Extended Data Figure 5 Reliability of the IP–MS methods); standardizing the signal intensity of the amyloid β-related peptide with the internal standard peptide to obtain a plurality of normalized intensities (see Plasma Aβ measurements and Extended Data Figure 5 Reliability of the IP–MS methods); and performing regression analysis on the plurality of normalized intensities and concentration of the amyloid β-related peptide (see Data Analysis and Extended Data Figure 5 Reliability of the IP–MS methods). Nakamura fails to disclose “providing a plurality of standard solutions containing the amyloid β-related peptide and a surfactant” as recited in the instant claim. Kaneko discloses a method for measuring a polypeptide in a biological sample (see abstract) using IP-MS, wherein the polypeptide is an amyloid β-related peptide (see [0043]). The method discloses providing a biological sample and a binding solution for performing IP (see [0052]), wherein the binding solution is a neutral surfactant having maltose, trehalose, and/or glucose in a hydrophilic part (i.e., nonionic) (see [0054]). Kaneko and Nakamura are analogous in the art of amyloid β-related peptide quantification. Therefore, it would have been obvious to one of ordinary skill in the art before the effective filing date to modify the method of Nakamura to add the surfactant of Kaneko to the sample containing the amyloid β-related peptide for the benefit of suppressing non-specific adsorption (see [0054] of Kaneko). Regarding claim 2 , the combination of references above render obvious the method of claim 1 the use of a nonionic surfactant (see [0054] of Kaneko). Regarding claim 3 , the combination of references above render obvious the method of claim 1 and wherein the amyloid β-related peptide is Aβ1-40, Aβ1-42, and/or APP669-711 (see Extended Data Figure 5 Reliability of the IP-MS methods of Nakamura). Regarding claim 4 , the combination of references above render obvious the invention of claim 1. Nakamura discloses wherein the immunoprecipitation and the mass spectrometry includes: incubating antibody beads (i.e., first carrier) with a plasma sample containing Aβ-related peptides and internal standard to bind said peptides (i.e., first bonding step resulting in first conjugate) (see Plasma Aβ measurements); a first washing step of washing the first conjugate (see Plasma Aβ measurements); a first elution step of eluting the bound peptides with glycine buffer having a pH of 2.8 (i.e., acidic solution) (see Plasma Aβ measurements); a neutralization step of mixing the first eluate with Tris buffer (i.e., neutral buffer) to obtain a purification solution with a pH of 7.4 (see Plasma Aβ measurements); repeating the immunoprecipitation steps (i.e., second bonding step and second washing step) and eluting the bound peptides with 70% acetonitrile containing 5 mM HCl (i.e., second elution step involving second acidic solution); and a detection step of detecting the amyloid β-related peptides in the second eluate by mass spectrometry (see Plasma Aβ measurements). Conclusion Any inquiry concerning this communication or earlier communications from the examiner should be directed to KATHRYN E LIMBAUGH whose telephone number is (571)272-0787. The examiner can normally be reached Monday-Thursday 7:00-5:00. 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, Lyle Alexander can be reached at (571) 272-1254. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300. Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000. /KATHRYN ELIZABETH LIMBAUGH/Primary Examiner, Art Unit 1797 Application/Control Number: 18/285,134 Page 2 Art Unit: 1797 Application/Control Number: 18/285,134 Page 3 Art Unit: 1797 Application/Control Number: 18/285,134 Page 4 Art Unit: 1797 Application/Control Number: 18/285,134 Page 5 Art Unit: 1797
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