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 .
Election/Restrictions
Applicants’ election without traversal of the disease to be treated being Alzheimer’s disease , the specific type of HSA being young and undamaged HSA, and the proposed property of the young and undamaged HSA having a lower level of carbonylation and the specific property of the young and undamaged HSA the level of carbonyl being lower than 1.7 mol/mg protein in the reply filed 23 March 2026.
Claims 15, 19-20, 22 and 25-32 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 23 March 2026.
Claims 12 and 16-18, 21 and 24 are under consideration.
Status of Claims
The claim listing filed 23 March 2026 is pending. Claims 15, 19-20, 22 and 25-32 are withdrawn from further consideration for the reasons set forth above, 37 CFR 1.142(b). Claims 12 and 16-18, 21, and 23-24 are being examined on the merits in this office action.
Priority
The present application claims status as a 371 (National Stage) of PCT/CN2021/127957 filed 1 November, 2021, and claims priority under 119(a)-(d) to Chinese Patent Application No. CN202011200484.6 filed 30 October 2020.
Receipt is acknowledged of certified copies of papers submitted under 35 USC 119(a)-(d) for Chinese Application No. CN202011200484.6, which papers have been placed of record in the file. Please note that the application is in Chinese and thus cannot be verified.
Please note that Applicants cannot rely upon the certified copy of the foreign priority application to overcome this rejection because a translation of said application has not been made of record in accordance with 37 CFR 1.55. When an English language translation of a non-English language foreign is required, the translation must be that of the certified copy (of the foreign application as filed) submitted together with a statement that the translation of the certified copy is accurate. See MPEP §§ 215 and 216.
Information Disclosure Statement
The Information Disclosure Statements (IDSs) submitted on 28 April 2023, 04 September 2024, and 23 April 2026 are in compliance with the provisions of 37 CFR 1.97. Accordingly, the Information Disclosure Statements are being considered by the examiner.
The listing of references in the specification is not a proper information disclosure statement. 37 CFR 1.98(b) requires a list of all patents, publications, or other information submitted for consideration by the Office, and MPEP § 609.04(a) states, "the list may not be incorporated into the specification but must be submitted in a separate paper." Therefore, unless the references have been cited by the examiner on form PTO-892, they have not been considered.
Claim Interpretation
The following terms recited in the claims have been interpreted according to the definitions provided in the specification, in accordance with the level of ordinary skill in the art. The specification states that the term "young and undamaged", as used in claim 12, means that the Human Serum Albumin (HSA) is in a fresh status and “has no significant damage”, and the specification gives an example of a “young individual” referring to a person “under the age of 30, preferably under the age of 18, more preferably under the age of 3, or even under the age of 1”. Under the broadest reasonable interpretation of the term “young and undamaged”, in view of the specification, the element of “young and undamaged” HSA is being interpreted as rHSA, with minimal medication, and without exposure to oxidation or proteolytic chemicals (i.e. sources of “damage” to a protein). The specification also states: “A skilled artisan will understand that the term "young and undamaged" HSA does not strictly require that there is absolutely no damage. It is very difficult, if not totally impossible, to prepare such perfect
preparations. For the purpose of the present invention, an HSA preparation comprising limited damages is still acceptable.” From the disclosure, under the broadest reasonable interpretation of the claim, any recombinantly-produced HSA meets this limitation of the preamble.
Claim Rejections - 35 USC § 112
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 17 and 24 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.
The term “compared to an endogenous HSA preparation obtained from a young individual of human” in claim 17 is a relative term with no accepted meaning in the art which renders the claim indefinite. The term “young individual of human” is not defined by the claim, the specification does not provide a standard for ascertaining the requisite degree, and one of ordinary skill in the art would not be reasonably apprised of the scope of the invention.
In the instant case, the invention is to a method of using human serum albumin (HSA) that exhibits “a lower level of carbonylation”, different to the level present in an endogenous HSA preparation. The claim is indefinite as there is no commonly accepted standard on which to base the comparison- the comparison being essential for setting forth the boundaries of the claim. Without a numeric standard, such as those provided in claims 18 and 21, there is no possible manner to determine if any given preparation of HSA fulfills the limitation.
The property chosen in the response to the restriction and election requirement filed 23 March 2026, in claim 1 also refers to a relative term, “lower”, which renders the claim indefinite. One of ordinary skill in the art would not be reasonably apprised of the scope of the invention.
Therefore, the metes and bounds of the claimed HSA preparation in claims 17 and 24 are indefinite, as the claimed properties are compared to another variable preparation, and not to any defined numeric value or to a common accepted standard in the art. See MPEP § 2173.05(b). II.
Claim Rejections - 35 USC § 102
The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
Claim 1 is rejected under 35 U.S.C. 102 (a)(1) as being anticipated by Stanyon and Viles, hereafter “Stanyon” (“Human serum albumin can regulate amyloid-β peptide fiber growth in the brain interstitium: implications for Alzheimer disease.” J Biol Chem. 2012 Aug 10;287(33):28163-8. doi: 10.1074/jbc.C112.360800. Epub 2012 Jun 20. PMID: 22718756; PMCID: PMC3431649.).
Regarding claim 12, Stanyon teaches that extracellular accumulation of amyloid-β peptide in the brain interstitium is a characteristic of Alzheimer’s disease and that Human Serum Albumin (HSA) is capable of regulating amyloid-β peptide fiber growth in the brain interstitium (pg. 28163, “Alzheimer disease is a neurodegenerative disorder characterized by extracellular accumulation of amyloid-β peptide (Aβ) in the brain interstitium.”; pg. 28166 “Our results show that at physiological levels of albumin, the rate at which fiber formation is nucleated for both Aβ(1–40) and Aβ(1–42) is significantly inhibited. Moreover the total concentration of fiber generated is reduced by HSA; this suggests that HSA binds to Aβ molecules and traps them in a nonfibrillar form so that they are not available to form fibers.”).
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 16 and 17 are rejected under 35 U.S.C. 103 as being unpatentable over Stanyon and Viles, hereafter “Stanyon” (“Human serum albumin can regulate amyloid-β peptide fiber growth in the brain interstitium: implications for Alzheimer disease.”), as applied to claim 1 above, and further in view of Jana et al., hereafter “Jana”, (“Specificity of age-related carbonylation of plasma proteins in the mouse and rat.” Archives of biochemistry and biophysics vol. 397,2 (2002): 433-9.).
Regarding claim 16, as stated above, Stanyon teaches the use of Human Serum Albumin (HSA) to regulate extracellular accumulation of amyloid-β peptide, a characteristic of Alzheimer’s disease (pg. 28166 “Our results show that at physiological levels of albumin, the rate at which fiber formation is nucleated for both Aβ(1–40) and Aβ(1–42) is significantly inhibited. Moreover the total concentration of fiber generated is reduced by HSA; this suggests that HSA binds to Aβ molecules and traps them in a nonfibrillar form so that they are not available to form fibers.”).
Stanyon does not teach the HSA being young and undamaged.
Jana teaches that in mice and Rhesus monkeys, the amount of carbonylation of plasma albumin increases with age, and states that this is a selective phenomenon (pg. 433 “In the rat, albumin and a 167-kDa protein, alpha1 macroglobulin (a-1M), showed significant age-dependent accrual of carbonylation. In the plasma of middle age Rhesus monkeys, in addition to albumin, a 54-kDa protein showed carbonylation. … Results of this study indicate that age-associated increase in protein carbonylation is a selective and not a random phenomenon. However, the set of proteins that become carbonylated differs in different species.”). Jana also suggests that carbonylated albumin can be a possible marker of oxidative damage in the plasma (pg. 438, “Since albumin was found to be carbonylated in the mouse and rat as well as monkey (albeit, examined at only one age), albumin can be suggested to be a possible general marker of oxidative damage in the plasma.”).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to combine the teachings of Stanyon and Jana to arrive at the instant invention due to Stanyon teaching the use of HSA to treat Alzheimer’s disease, and Jana teaching that young and undamaged HSA performs better than its counterpart and that carbonylation of albumin has an age-associated increase.
One would have recognized from Stanyon that administering HSA in the treatment of Alzheimer’s disease would be beneficial. One would also have been motivated to seek a version of HSA that according to BRI, the inclusion of the HSA of Jana having a lower level of carbonylation means that it meets the limitation set forth in “young and undamaged”. Hence the combination of references would have been readily apparent and deemed to be a mere (A) Combining prior art elements according to known methods to yield predictable results (see MPEP 2143(I)).
Regarding claim 17, as stated above, Stanyon teaches the use of Human Serum Albumin (HSA) to regulate extracellular accumulation of amyloid-β peptide, a characteristic of Alzheimer’s disease (pg. 28166 “Our results show that at physiological levels of albumin, the rate at which fiber formation is nucleated for both Aβ(1–40) and Aβ(1–42) is significantly inhibited. Moreover the total concentration of fiber generated is reduced by HSA; this suggests that HSA binds to Aβ molecules and traps them in a nonfibrillar form so that they are not available to form fibers.”).
Stanyon does not teach the HSA being young and undamaged and the HSA exhibiting a lower level of carbonylation.
Jana teaches that in mice and Rhesus monkeys, the amount of carbonylation of plasma albumin increases with age, and states that this is a selective phenomenon (pg. 433 “In the rat, albumin and a 167-kDa protein, alpha1 macroglobulin (a-1M), showed significant age-dependent accrual of carbonylation. In the plasma of middle age Rhesus monkeys, in addition to albumin, a 54-kDa protein showed carbonylation. … Results of this study indicate that age-associated increase in protein carbonylation is a selective and not a random phenomenon. However, the set of proteins that become carbonylated differs in different species.”). Jana also suggests that carbonylated albumin can be a possible marker of oxidative damage in the plasma (pg. 438, “Since albumin was found to be carbonylated in the mouse and rat as well as monkey (albeit, examined at only one age), albumin can be suggested to be a possible general marker of oxidative damage in the plasma.”).
Claims 18, 21 and 23 are rejected under 35 U.S.C. 103 as being unpatentable over Stanyon and Viles, hereafter “Stanyon” (“Human serum albumin can regulate amyloid-β peptide fiber growth in the brain interstitium: implications for Alzheimer disease.”) and Jana et al., hereafter “Jana”, (“Specificity of age-related carbonylation of plasma proteins in the mouse and rat.” Archives of biochemistry and biophysics vol. 397,2 (2002): 433-9), as applied to claim 16 above, and further in view of Himmelfarb and McMonagle, hereafter “Himmelfarb” ("Albumin is the major plasma protein target of oxidant stress in uremia." Kidney International, Volume 60, Issue 1, 2001, Pages 358-363, ISSN 0085-2538, https://doi.org/10.1046/j.1523-1755.2001.00807.x.) and Amsbio (“Protein carbonyl content assay kit.” (2012, January). https://resources.amsbio.com/Datasheets/K830-100.pdf).
Regarding claim 18, as stated above, Stanyon teaches the use of Human Serum Albumin (HSA) to regulate extracellular accumulation of amyloid-β peptide, a characteristic of Alzheimer’s disease (pg. 28166 “Our results show that at physiological levels of albumin, the rate at which fiber formation is nucleated for both Aβ(1–40) and Aβ(1–42) is significantly inhibited. Moreover the total concentration of fiber generated is reduced by HSA; this suggests that HSA binds to Aβ molecules and traps them in a nonfibrillar form so that they are not available to form fibers.”).
Jana teaches that in mice and Rhesus monkeys, the amount of carbonylation of plasma albumin increases with age, and states that this is a selective phenomenon (pg. 433 “In the rat, albumin and a 167-kDa protein, alpha1 macroglobulin (a-1M), showed significant age-dependent accrual of carbonylation. In the plasma of middle age Rhesus monkeys, in addition to albumin, a 54-kDa protein showed carbonylation. … Results of this study indicate that age-associated increase in protein carbonylation is a selective and not a random phenomenon. However, the set of proteins that become carbonylated differs in different species.”). Jana also suggests that carbonylated albumin can be a possible marker of oxidative damage in the plasma (pg. 438, “Since albumin was found to be carbonylated in the mouse and rat as well as monkey (albeit, examined at only one age), albumin can be suggested to be a possible general marker of oxidative damage in the plasma.”).
Stanyon and Jana do not teach the HSA exhibiting a level of carbonylation lower than 1.7 nmol/mg protein.
Himmelfarb teaches that when compared to patients with chronic renal failure (CRF), healthy volunteers had a lower protein carbonyl concentration, specifically one below 1.7nmol/mg protein (pg. 361, “Patients with CRF (range of creatinine clearance 16 to 46 mL/min) had a significantly elevated total plasma protein carbonyl concentration compared with healthy volunteers (0.31 ± 0.07 nmol per mg protein in CRF patients vs. 0.04 ± 0.01 nmol per mg protein healthy volunteers, P < 0.001; Figure 4)”).
Stanyon, Jana, and Himmelfarb do not teach the use of a Protein Carbonyl Content Assay Kit to determine the carbonyl level of the HSA.
Amsbio teaches a kit used to quantify protein carbonylation, while also teaching that the kit provides a simple and accurate method of quantification (pg. 1, “Protein carbonyl groups are an important and immediate biomarker of oxidative stress. … BioVision’s Protein Carbonyl Content Assay Kit is designed to provide a simple and accurate method of quantifying carbonyls in protein samples.”).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to combine the teachings of Stanyon, Jana, Himmelfarb and Amsbio to arrive at the presently claimed invention due to Stanyon teaching the use of HSA to treat Alzheimer’s disease, Jana teaching that young and undamaged HSA performs better than its counterpart and that carbonylation of albumin has an age-associated increase, Himmelfarb teaching that healthy patients tend to have a carbonylation level below 1.7 nmol/mg and Amsbio teaching a method of determining protein carbonyl content.
One would have recognized from Stanyon that administering HSA in the treatment of Alzheimer’s disease would be beneficial. One would also have been motivated to seek a version of HSA that according to BRI, the inclusion of the HSA of Jana having a lower level of carbonylation means that it meets the limitation set forth in “young and undamaged”. The ordinarily skilled artisan would also take the teaching of healthy subjects having a level of carbonylation lower than 1.7 nmol/mg, as taught by Himmelfarb, and the method of quantifying protein carbonylation as taught by Amsbio and have a reason to combine them due to Stanyon and Jana teaching the use and a property of young HSA being low carbonylation and combining it with the teachings of Himmelfarb and Amsbio due to them teaching a low level of carbonylation (according to the BRI of the claimed invention, a low level of carbonylation is a characteristic of “young and undamaged” HSA) and a method of quantifying it. Hence the combination of references would have been readily apparent and deemed to be a mere (A) Combining prior art elements according to known methods to yield predictable results (see MPEP 2143(I)).
Regarding claim 21, Himmelfarb teaches that when compared to patients with chronic renal failure (CRF), healthy volunteers had a lower protein carbonyl concentration, specifically one below 1.5 nmol/mg protein (pg. 361, “Patients with CRF (range of creatinine clearance 16 to 46 mL/min) had a significantly elevated total plasma protein carbonyl concentration compared with healthy volunteers (0.31 ± 0.07 nmol per mg protein in CRF patients vs. 0.04 ± 0.01 nmol per mg protein healthy volunteers, P < 0.001; Figure 4)”).
Regarding claim 23, Himmelfarb teaches that when compared to patients with chronic renal failure (CRF), healthy volunteers had a lower protein carbonyl concentration, specifically one below 1.5 nmol/mg protein (pg. 361, “Patients with CRF (range of creatinine clearance 16 to 46 mL/min) had a significantly elevated total plasma protein carbonyl concentration compared with healthy volunteers (0.31 ± 0.07 nmol per mg protein in CRF patients vs. 0.04 ± 0.01 nmol per mg protein healthy volunteers, P < 0.001; Figure 4)”).
Claim 24 is rejected under 35 U.S.C. 103 as being unpatentable over Stanyon and Viles, hereafter “Stanyon” (“Human serum albumin can regulate amyloid-β peptide fiber growth in the brain interstitium: implications for Alzheimer disease.”) and Jana et al., hereafter “Jana”, (“Specificity of age-related carbonylation of plasma proteins in the mouse and rat.” Archives of biochemistry and biophysics vol. 397,2 (2002): 433-9), as applied to claim 17 above, and further in view of Chen et al., hereafter “Chen”, ("Human serum albumin from recombinant DNA technology: Challenges and strategies.", Biochimica et Biophysica Acta (BBA) - General Subjects, Volume 1830, Issue 12, 2013, Pages 5515-5525, ISSN 0304-4165, https://doi.org/10.1016/j.bbagen.2013.04.037.).
Regarding claim 24, Chen teaches that there is a shortage of and safety issues arising from the use of plasma (pg. 1“As the most abundant protein in the blood, human serum albumin (HSA) plays an important role in maintaining plasma oncotic pressure and fluid balance between the body's compartments. HSA is thus widely used in the clinic to treat diseases. However, the shortage of and safety issues arising from using plasma HSA (pHSA) underscore the importance of recombinant HSA (rHSA) as a promising substitute for pHSA.”). Chen also teaches that recombinant HSA (rHSA) is cost-effective and safe (pg. 1, “rHSA can be highly expressed in various hosts and seems to be identical to pHSA. rHSA generated from yeast appears to be as efficient and safe as pHSA in a series of preclinical and clinical trials, whereas rHSA from rice seeds exhibits great potential for more cost-effective production.”).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to combine the teachings of Stanyon, Jana, and Chen to arrive at the instant invention due to Stanyon teaching the use of HSA to treat Alzheimer’s disease, and Jana teaching that young and undamaged HSA performs better than its counterpart and that carbonylation of albumin has an age-associated increase, and Chen teaching that rHSA generated from yeast and rice seed are efficient and safe (yeast) and rHSA generated from rice seeds is cost effective.
One would have recognized from Stanyon that administering HSA in the treatment of Alzheimer’s disease would be beneficial. One would also have been motivated to seek a version of HSA that according to BRI, the inclusion of the HSA of Jana having a lower level of carbonylation means that it meets the limitation set forth in “young and undamaged”. The ordinarily skilled artisan would be motivated to have the HSA produced recombinantly due to Chen teaching that RHSA is a cost-effective way to receive the same results as plasma derived HSA. Hence the combination of references would have been readily apparent and deemed to be a mere (A) Combining prior art elements according to known methods to yield predictable results (see MPEP 2143(I)).
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.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
Claims 12, 16-18, 21, and 23-24 provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claim 1, 6, 8 and 9 of copending Application No. 18/041,319 (claim listing filed 17 March 2026), in view of Stanyon and Viles, hereafter “Stanyon” (“Human serum albumin can regulate amyloid-β peptide fiber growth in the brain interstitium: implications for Alzheimer disease.” J Biol Chem. 2012 Aug 10;287(33):28163-8. doi: 10.1074/jbc.C112.360800. Epub 2012 Jun 20. PMID: 22718756; PMCID: PMC3431649.). Although the claims at issue are not identical, they are not patentably distinct from each other because the instant application recites a method of using the composition of ‘319.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Regarding claim 12, ‘319 recites a preparation of young and undamaged human serum albumin (HSA) that exhibits at least three or all of the following properties:(1) a ratio of free thiol in Cys-34 residue being greater than 50%, as determined by Ellman's method; (2) a level of advanced glycation end-product (AGE) being lower than 60 pq/q protein, as determined by ELISA; (3) a level of carbonyl lower than 1.7 nmol/mg protein, as determined by Protein Carbonyl Content Assay Kit; and (4) a level of homocysteinylation lower than 5 nmol/g protein as determined by ELISA; wherein the ratio of free thiol in Cys-34 residue means: the ratio of the concentration of HSA with reduced Cys-34 residue in the preparation to the total concentration of HSA in the preparation; and wherein the position of Cys-34 residue is determined based on the amino acid sequence of wild type HSA (See claim 1).
‘319 does not recite the use of the composition.
Stanyon teaches that extracellular accumulation of amyloid-β peptide in the brain interstitium is a characteristic of Alzheimer’s disease and that Human Serum Albumin (HSA) is capable of regulating amyloid-β peptide fiber growth in the brain interstitium (pg. 28163, “Alzheimer disease is a neurodegenerative disorder characterized by extracellular accumulation of amyloid-β peptide (Aβ) in the brain interstitium.”; pg. 28166 “Our results show that at physiological levels of albumin, the rate at which fiber formation is nucleated for both Aβ(1–40) and Aβ(1–42) is significantly inhibited. Moreover the total concentration of fiber generated is reduced by HSA; this suggests that HSA binds to Aβ molecules and traps them in a nonfibrillar form so that they are not available to form fibers.”).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to use the composition comprising HSA as described in claim 1 of ‘319 because the claims teach a preparation of HSA, which was show to be used to treat Alzheimer’s disease. The claimed invention is drawn to the use of an HSA preparation. One of ordinary skill in the before the effective filing date of the claimed invention would be motivated with reasonable expectation of success to use the preparation comprising HSA of ‘319 to treat Alzheimer’s disease as described in Stanyon due to both ‘319 and Stanyon teaching HSA, and Stanyon teaching that HSA can be used to regulate amyloid-β peptide fiber growth in the brain interstitium.
Regarding claim 18, ‘319 teaches the level of carbonyl being lower than 1.7 nmol/mg protein (See claim 1).
Regarding claims 21 and 23, ‘319 teaches the level of carbonyl being lower than 1.5 nmol/mg protein (See claim 6 and 8).
Regarding claim 24, ‘319 teaches the composition being produced recombinantly (See claim 9).
Status of Claims
Claims 12, 16-18, 21 and 23-24 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph. Claim 12 is rejected under 35 U.S.C. 102 (a)(1). Claims 16-18, 21 and 23-24 are rejected under 35 U.S.C. 103. Claims 12, 16-18, 21 and 23-24 are rejected on the ground of nonstatutory
double patenting.
No claims are allowed.
Conclusion
Any inquiry concerning this communication or earlier communications from the examiner should be directed to Daliyah M. Brown whose telephone number is (571)272-0136. The examiner can normally be reached Monday-Thursday 9:00 am - 4:30 pm.
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/Daliyah M. Brown/Examiner, Art Unit 1654
/LIANKO G GARYU/Supervisory Patent Examiner, Art Unit 1654
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