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 .
Status of the Claims
1. Claims 1-20 are the original claims filed 8/4/2023. In the Reply filed 3/5/2026, Claims 1, 9, 15 and 20 are amended. Claims 1-20 are of the claims.
Election/Restrictions
2. Applicant’s election of Group I in the reply filed on 3/5/2026 is acknowledged. Because applicant did not distinctly and specifically point out the supposed errors in the restriction requirement, the election has been treated as an election without traverse (MPEP § 818.01(a)).
3. Claims 15-19 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention, there being no allowable generic or linking claim.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 3/5/2026.
4. Claims 1-14 and 20 are the claims under examination.
Priority
5. USAN 18/365,239, filed 08/04/2023, is a Continuation of PCT/CN2022/074716, filed 01/28/2022, and claims foreign priority to CN 202110164375.1, filed 02/05/2021. Receipt is acknowledged of a certified copy of papers for CN 202110164375.1 as required by 37 CFR 1.55.
Information Disclosure Statement
6. As of 4/27/2026, a total of one (1) IDS is filed for this application: 8/4/2023. The corresponding initialed and dated 1449 form is considered and of record.
Objections
Specification
7. The disclosure is objected to because of the following informalities:
a) The figure legends for Figures 1-16 provide no identification of the panels shown in the corresponding figure (the panels are not labeled as, e.g., a, b, etc.) nor do they include a summary of the results or an explanation of what is shown in the figure.
b) The specification fails to include sequence identifiers for the peptide sequences > 4 amino acids in length at [0040; 0043; 0094; 0096] and pursuant to 37 CFR 1.812-1.825.
c) The use of the term Microfuge, SnapGene, CutSmart, which is a trade name or a mark used in commerce, has been noted in this application. The term should be accompanied by the generic terminology; furthermore the term should be capitalized wherever it appears or, where appropriate, include a proper symbol indicating use in commerce such as ™, SM , or ® following the term.
Although the use of trade names and marks used in commerce (i.e., trademarks, service marks, certification marks, and collective marks) are permissible in patent applications, the proprietary nature of the marks should be respected and every effort made to prevent their use in any manner which might adversely affect their validity as commercial marks.
Appropriate correction is required.
Claim Objections
8. Claims 1-14 and 20 are objected to because of the following informalities:
a) Claims 1-14 and 20 are replete with grammatical and idiomatic errors. The claims contain improper punctuation throughout (i.e., series of semicolons (;) preceded by a comma instead of a colon (i.e., “:”).
b) Claim 1 is missing the term “wherein” that is used to specify a particular effect, result, or characteristic produced by the already-recited elements of the claimed invention, and that serves to refine or further limit the scope of a claim by functioning to provide material technical details.
c) Claims 1-14 and 20 use improper transitional language throughout that should be replaced with comprises/comprising or consists of/consisting of. See MPEP 2111.03.
d) Claims 1-14 and 20 recite the phrase “the single-chain antibody fragment has an ability to specifically recognize and bind to an antigen” in claim 1. The recitation “ability” implies that some undefined structure or condition is what predicates whether specific recognition and binding does or does not occur. Ability suggests that the specific recognition and binding may sometimes occur but not always, and what determines the degree or amount of specific recognition and binding is not defined by the use of those term.
e) Claim 2 is seemingly drawn to the single-chain antibody fragment that binds to a human or non-human antigen recited in the Markush-like grouping. Clarification is required.
f) Amend claim 3 to recite “wherein
g) Amend claim 6 for consistency to use either brackets or parentheses around the peptide sequences but not both.
h) Amend claim 7 to delete the species “VL-VH-AC, VL-VH-AN, VH-VL-AC, VH-VL-AN” that do not define the relationship of L with the corresponding structure.
i) Amend claim 8 to recite “wherein he nano-assembly comprises at least two recombinant fusion proteins.
j) Amend Claim 13 to recite “[7200] 7,200” and “[110000] 110,000”.
k) Amend claim 15 into a pharmaceutical composition comprising an active ingredient of the nano-assembly of claim 1 and a drug specific for a tumor, an autoimmune disease, an inflammatory disease or an infection.
Appropriate correction is required.
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.
9. Claims 1-14 and 20 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.
a) Claims 1-14 and 20 are generally narrative and indefinite, failing to conform with current U.S. practice. They appear to be a literal translation into English from a foreign document and are replete with grammatical and idiomatic errors.
b) Claims 1-14 and 20 recite the limitation "or the fusion proteins with the intact hydrophobic domains which derived through substitution, deletion, and/or addition of one or more amino acids " in claim 1. There is insufficient antecedent basis for this limitation in the claims. The meaning of “the intact hydrophobic domains” is unclear. The claim is seemingly directed to a derivative comprising substitution, deletion, and/or addition of one or more amino acids for an intact hydrophobic domain and for which there is no antecedent basis.
c) Claim 5 is indefinite for the phrase “wherein VL is an antibody light chain variable region, peptide or polypeptide sequence, and VH is an antibody heavy chain variable region, peptide or polypeptide sequence, therapeutic protein and its fragments.” The meaning of a light chain peptide or polypeptide is unclear. The meaning of a heavy chain peptide or polypeptide is unclear. Antibody light and heavy chain variable regions are well known in the art and fragments thereof. What comprises a peptide or polypeptide sequence is unknown.
d) Claim 6 is indefinite for reciting a peptide sequence > 4 amino acids in length that is required to be identified by sequence identifier. MPEP 2422 or 37 CFR 1.821(d).
e) Claims 8-9 recite the limitation "recombinant fusion proteins" in claim 8. There is insufficient antecedent basis for this limitation in the claim. Claim 1 from which claims 8-9 depend does not recite much less define a recombinant fusion protein.
f) Claim 9 in depending from claim 8 is indefinite of the phrase “wherein the recombinant fusion protein comprises two or three types.” It is not ascertainable which of the at least two recombinant fusion proteins of claim 8 are being referred to. The meaning of “types” is indefinite and without antecedent basis as well.
g) A broad range or limitation together with a narrow range or limitation that falls within the broad range or limitation (in the same claim) may be considered indefinite if the resulting claim does not clearly set forth the metes and bounds of the patent protection desired. See MPEP § 2173.05(c). In the present instance, claim 11 recites the broad recitation “polylactide”, and the claim also recites “poly(L-lactide), poly(R-lactide), or a racemic polylactide; an end group of the polylactide is at least one of ester, carboxyl, and hydroxyl groups”, which is the narrower statement of the range/limitation.
At least based on claim 12, clarification is provided for the poly(L-lactide) and the end group of the poly(L-lactide) is an ester group.
The claim(s) are considered indefinite because there is a question or doubt as to whether the feature introduced by such narrower language is (a) merely exemplary of the remainder of the claim, and therefore not required, or (b) a required feature of the claims.
h) Claim 11 is indefinite for the phrase “poly(L-lactide), poly(R-lactide), or a racemic polylactide; an end group of the polylactide is at least one of ester, carboxyl, and hydroxyl groups”. The claim omits conjunctive or disjunctive language and the POSA cannot reasonably ascertain the full metes and bounds of the claim.
Claim Rejections - 35 USC § 103
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.
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.
10. Claims 1-2, 5, 8-14 and 20 are rejected under 35 U.S.C. 103(a) as being unpatentable over Marquette et al (US 20160090415; filed 2014-05-21) as evidenced by Feige et al (Trends Biochem Sci. 2009 Dec 21;35(4):189–198).
The common technical feature of a nano-assembly comprised within a nanoparticle, wherein the nano-assembly comprises a polyester and a protein comprising a hydrophobic domain, e.g., albumin, wherein the hydrophobic domain of the protein is bound with the polyester through hydrophobic interactions, wherein the protein further comprises a single chain antibody fragment with binding ability for an antigen that when combined with other proteins of the invention generates a multi-specific antibody forming a nano-assembly comprised within the nanoparticle is prima facie obvious over Marquette, Irvine and Yu.
AS regards claims 1, 5, and 10-11, Marquette teaches forming nanoparticles with PLGA (polymers between polylactic and polyglycolide) and IgG (Examples, p. 6-8), where the VH/VL of the Fab portion of the IgG comprises the immunoregulatory functional fragment and the constant regions comprises a hydrophobic region. The IgG of Marquette inherently comprises a hydrophobic region in specifically the constant domains that make up the immunoglobulin (Ig) fold (CH1, CH2, CH3 and CL), and that comprise a central, hydrophobic core (region) that stabilizes the protein as evidenced by Feige (PTO 892). Where Marquette teaches multispecific antibodies comprising the nanoparticle, then the assembly necessarily contains at least 5 hydrophobic regions.
Given that the PLGA nanoparticles by definition comprise polyester and that IgG reads on a protein, the limitations of “a nano-assembly” of claim 1 are met.
AS regards claim 2, Marquette teaches the same antigen for the protein at
[0076] Preferred molecular targets for antibodies encompassed by the present invention include CD polypeptides such as CD3, CD4, CD8, CD19, CD20, CD22, CD23, CD30, CD34, CD38, CD40, CD80, CD86, CD95 and CD154; members of the HER receptor family such as the EGF receptor, HER2, HER3 or HER4 receptor; cell adhesion molecules such as LFA-1, Mac1, p150,95, VLA-4, ICAM-1, VCAM and av/b3 integrin including either α or β subunits thereof (e.g. anti-CD11 a, anti-CD18 or anti-CD11 b antibodies); chemokines and cytokines or their receptors such as IL-1 α and β, IL-2, IL-6, the IL-6 receptor, IL-12, IL-13, IL-17 forms, IL-18, IL-21, IL-23, IL-25, IL-27, TNFα and TNFβ; growth factors such as VEGF; IgE; blood group antigens; flk2/flt3 receptor; obesity (OB) receptor; mp1 receptor; CTLA-4; polypeptide C; G-CSF, G-CSF receptor, GM-CSF, GM-CSF receptor, M-CSF, M-CSF receptor; LINGO; BAFF, APRIL; OPG; OX40; OX40-L; and FcRn.
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AS regards claims 8-9, Marquette teaches multispecific antibodies at
[0067] single-chain antibodies; bispecific, trispecific, tetraspecific or multispecific antibodies formed from antibody fragments or antibodies..”
AS regards claim 11, Marquette teaches the polyactides at
[0072] The term “polymer” as used herein refers to a chemical compound or mixture of compounds consisting of repeating structural units created through a process of polymerization, from which originates a characteristic of high relative molecular mass and attendant properties. Generally, the units composing polymers derive, actually or conceptually, from molecules of low relative molecular mass. For the purposes of drug delivery, thermoplastic aliphatic poly(esters), such as poly-lactide (PLA), poly-glycolide (PGA), and especially PLGA, are useful polymers due to excellent biocompatibility and biodegradability.
AS regards claim 12, Marquette teaches thermoplastic aliphatic poly(esters) at
[0006] Thermoplastic aliphatic poly(esters), such as poly-lactide [PLA], poly-glycolide [PGA], and especially poly(D,L-lactide-co-glycolide) [PLGA] have generated tremendous interest due to their excellent biocompatibility and biodegradability.
[0072] The term “polymer” as used herein refers to a chemical compound or mixture of compounds consisting of repeating structural units created through a process of polymerization, from which originates a characteristic of high relative molecular mass and attendant properties. Generally, the units composing polymers derive, actually or conceptually, from molecules of low relative molecular mass. For the purposes of drug delivery, thermoplastic aliphatic poly(esters), such as poly-lactide (PLA), poly-glycolide (PGA), and especially PLGA, are useful polymers due to excellent biocompatibility and biodegradability.
AS regards claims 13-14, Marquette teaches the lower range of nanoparticles to be about 300nm ([0070]). Moreover, the PLGA size of 7,200 to 1,100,000 Da is included as the size fraction of diafiltration is done with 15-30K membrane (note examples).
As regards claim 20 (interpreted as a pharmaceutical composition), Marquette teaches the nanoparticles are available for drug loading (e.g. drug delivery) of various antibodies (p.5-6, [0076]).
The motivation to produce a nano-assembly comprised within a nanoparticle is because of a need for polymer matrix-based nanoparticles comprising antibodies or other therapeutic, diagnostic or preventive proteins having: controlled release; and an increased encapsulation efficiency. The reference defines the materials and reagents with sufficient detail in order to make and use a nano-assembly complexed-nanoparticle with a reasonable degree of predictability and an assurance of success because of the limited number of reagents, the availability of the reagents, and the steps for producing the nano-assembly complexed-nanoparticle.
11. Claim(s) 1 and 4 is/are rejected under 35 U.S.C. 103 as being unpatentable over Marquette et al (US 20160090415; filed 2014-05-21) as evidenced by Feige et al (Trends Biochem Sci. 2009 Dec 21;35(4):189–198) and as applied to claim 1 above, and further in view of Irvine et al (US 20140377334; filed 2014-06-19).
Claim 4 is drawn to the nano-assembly of claim 1 within a nanoparticle where the hydrophobic region is albumin is prima facie obvious over Marquette in view of Irvine.
As regards claim 1, Marquette teaches forming nanoparticles with PLGA (polymers between polylactic and polyglycolide) and IgG (Examples, p. 6-8), where the VH/VL of the Fab portion of the IgG comprises the immunoregulatory functional fragment and the constant regions comprises a hydrophobic region. The IgG of Marquette inherently comprises a hydrophobic region in specifically the constant domains that make up the immunoglobulin (Ig) fold (CH1, CH2, CH3 and CL), and that comprise a central, hydrophobic core (region) that stabilizes the protein as evidenced by Feige (PTO 892). Where Marquette teaches multispecific antibodies comprising the nanoparticle, then the assembly necessarily contains at least 5 hydrophobic regions.
Irvine teaches use of IL-2-Fc antibody with therapeutic antibody and PLGA nanoparticles (p. 5-7) including CD137, CTLA-4 and PD-1 pairs ([0090]). Irvine teaches using smaller size nanoparticles to facilitate distribution, and the use of Fc antibody improves targeting (Fig).
As regards claim 4, Irvine teaches formation of nanoparticles comprising polymers comprising hydrophobic proteins such as albumin at
[0105] In some embodiments, particles of the present disclosure are formed from polymers including, without limitation, aliphatic polyesters, poly (lactic acid) (PLA), poly (glycolic acid) (PGA), co-polymers of lactic acid and glycolic acid (PLGA), polycarprolactone (PCL), polyanhydrides, poly(ortho)esters, polyurethanes, poly(butyric acid), poly(valeric acid), and poly(lactide-co-caprolactone), and natural polymers such as alginate and other polysaccharides including dextran and cellulose, collagen, chemical derivatives thereof, including substitutions, additions of chemical groups such as for example alkyl, alkylene, hydroxylations, oxidations, and other modifications routinely made by those skilled in the art), albumin and other hydrophilic proteins, zein and other prolamines and hydrophobic proteins, copolymers and mixtures thereof.
The motivation to produce a nano-assembly comprised within a nanoparticle is because of a need for polymer matrix-based nanoparticles comprising antibodies or antigen binding fragments, polymers comprising aliphatic polyesters, and albumin and other hydrophilic proteins having: controlled release; and an increased encapsulation efficiency. The reference defines the materials and reagents with sufficient detail in order to make and use a nano-assembly complexed-nanoparticle with a reasonable degree of predictability and an assurance of success because of the limited number of reagents, the availability of the reagents, and the steps for producing the nano-assembly complexed-nanoparticle.
12. Claims 1-14 and 20 is/are rejected under 35 U.S.C. 103 as being obvious over U.S. Patent No. 11957764 (filed 2020/10/21) in view of Marquette et al (US 20160090415; filed 2014-05-21).
The applied reference has a common assignee with the instant application. Based upon the earlier effectively filed date of the reference, it constitutes prior art under 35 U.S.C. 102(a)(2).
Although the claims at issue are not identical, they are not patentably distinct from each other because the claims share the common technical feature of a nano-assembly comprised within a nanoparticle, wherein the nano-assembly comprises a polyester and a protein comprising a hydrophobic domain, e.g., albumin, wherein the hydrophobic domain of the protein is bound with the polyester through hydrophobic interactions, wherein the protein further comprises a single chain antibody fragment with binding ability for an antigen that when combined with other proteins of the invention generates a multi-specific antibody forming a nano-assembly comprised within the nanoparticle. The reference patent claims anticipate and render obvious the scope of the instant claimed.
Ref claims
1. A multi-specific antibody delivery platform, which is formed by bonding a protein-type nanoparticle with an anti-Fc antibody through a chemical bond, wherein the protein-type nanoparticle includes polyester and a protein with a hydrophobic domain, and the hydrophobic domain of the protein is bound with the polyester through hydrophobic interaction, wherein the protein is albumin or a cell wall protein, and the protein has a same species as a recipient of the delivered specific antibody, wherein the anti-Fc antibody is an anti-IgG-Fc antibody; a weight ratio of the polyester to the protein is within a range of 1:(9-11); a Fab domain of the anti-Fc antibody is non-covalently bound with an Fc domain of a delivered specific antibody; and the delivered specific antibody has a same species as an Fc segment recognized by the anti-Fe antibody.
2. The multi-specific antibody delivery platform of claim 1, wherein the protein is at least one of a human serum albumin, a bovine serum albumin, a mouse serum albumin, an ovalbumin, a protein A, or protein G.
3. The multi-specific antibody delivery platform of claim 1, wherein the polyester is aliphatic polyester or polyethylene glycol-modified aliphatic polyester.
4. The multi-specific antibody delivery platform of claim 3, wherein the aliphatic polyester is at least one of polylactic acid, polyglycolide, poly(glycolide-co-lactide), or polycaprolactone; and the polyethylene glycol-modified aliphatic polyester is at least one of polyethylene glycol-modified polylactic acid, polyethylene glycol-modified polyglycolide, polyethylene glycol-modified poly(glycolide-co-lactide), or polyethylene glycol-modified polycaprolactone.
5. The multi-specific antibody delivery platform of claim 4, wherein the aliphatic polyester is polylactic acid; the polylactic acid is L-polylactic acid, D-polylactic acid, or racemic polylactic acid; and a terminal group of the polylactic acid is at least one of an ester group, a carboxyl group, or a hydroxyl group.
6. The multi-specific antibody delivery platform of claim 5, wherein the polylactic acid is the L-polylactic acid, a terminal group of the L-polylactic acid is the ester group, and a molecular weight of the L-polylactic acid is within a range of 7200 Daltons-1100000 Daltons.
7. The multi-specific antibody delivery platform of claim 4, wherein a ratio of LA/GA in the poly(glycolide-co-lactide) is within a range of 95/5-50/50.
8. The multi-specific antibody delivery platform of claim 1, wherein an average particle size of the protein-type nanoparticle is within a range of 100 nm to 200 nm.
9. The multi-specific antibody delivery platform of claim 1, wherein the multi-specific antibody delivery platform delivers at least two specific antibodies.
10. A mufti-specific antibody delivery system, comprising the multi-specific antibody delivery platform of claim 1 and a specific antibody.
AS regards claims 1, 5, and 10-11, Marquette teaches forming nanoparticles with PLGA (polymers between polylactic and polyglycolide) and IgG (Examples, p. 6-8), where the VH/VL of the Fab portion of the IgG comprises the immunoregulatory functional fragment and the constant regions comprises a hydrophobic region. The IgG of Marquette inherently comprises a hydrophobic region in specifically the constant domains that make up the immunoglobulin (Ig) fold (CH1, CH2, CH3 and CL), and that comprise a central, hydrophobic core (region) that stabilizes the protein as evidenced by Feige (PTO 892). Where Marquette teaches multispecific antibodies comprising the nanoparticle, then the assembly necessarily contains at least 5 hydrophobic regions.
Given that the PLGA nanoparticles by definition comprise polyester and that IgG reads on a protein, the limitations of “a nano-assembly” of claim 1 are met.
AS regards claim 2, Marquette teaches the same antigen for the protein at
[0076] Preferred molecular targets for antibodies encompassed by the present invention include CD polypeptides such as CD3, CD4, CD8, CD19, CD20, CD22, CD23, CD30, CD34, CD38, CD40, CD80, CD86, CD95 and CD154; members of the HER receptor family such as the EGF receptor, HER2, HER3 or HER4 receptor; cell adhesion molecules such as LFA-1, Mac1, p150,95, VLA-4, ICAM-1, VCAM and av/b3 integrin including either α or β subunits thereof (e.g. anti-CD11 a, anti-CD18 or anti-CD11 b antibodies); chemokines and cytokines or their receptors such as IL-1 α and β, IL-2, IL-6, the IL-6 receptor, IL-12, IL-13, IL-17 forms, IL-18, IL-21, IL-23, IL-25, IL-27, TNFα and TNFβ; growth factors such as VEGF; IgE; blood group antigens; flk2/flt3 receptor; obesity (OB) receptor; mp1 receptor; CTLA-4; polypeptide C; G-CSF, G-CSF receptor, GM-CSF, GM-CSF receptor, M-CSF, M-CSF receptor; LINGO; BAFF, APRIL; OPG; OX40; OX40-L; and FcRn.
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AS regards claims 8-9, Marquette teaches multispecific antibodies at
[0067] single-chain antibodies; bispecific, trispecific, tetraspecific or multispecific antibodies formed from antibody fragments or antibodies..”
AS regards claim 11, Marquette teaches the polyactides at
[0072] The term “polymer” as used herein refers to a chemical compound or mixture of compounds consisting of repeating structural units created through a process of polymerization, from which originates a characteristic of high relative molecular mass and attendant properties. Generally, the units composing polymers derive, actually or conceptually, from molecules of low relative molecular mass. For the purposes of drug delivery, thermoplastic aliphatic poly(esters), such as poly-lactide (PLA), poly-glycolide (PGA), and especially PLGA, are useful polymers due to excellent biocompatibility and biodegradability.
AS regards claim 12, Marquette teaches thermoplastic aliphatic poly(esters) at
[0006] Thermoplastic aliphatic poly(esters), such as poly-lactide [PLA], poly-glycolide [PGA], and especially poly(D,L-lactide-co-glycolide) [PLGA] have generated tremendous interest due to their excellent biocompatibility and biodegradability.
[0072] The term “polymer” as used herein refers to a chemical compound or mixture of compounds consisting of repeating structural units created through a process of polymerization, from which originates a characteristic of high relative molecular mass and attendant properties. Generally, the units composing polymers derive, actually or conceptually, from molecules of low relative molecular mass. For the purposes of drug delivery, thermoplastic aliphatic poly(esters), such as poly-lactide (PLA), poly-glycolide (PGA), and especially PLGA, are useful polymers due to excellent biocompatibility and biodegradability.
AS regards claims 13-14, Marquette teaches the lower range of nanoparticles to be about 300nm ([0070]). Moreover, the PLGA size of 7,200 to 1,100,000 Da is included as the size fraction of diafiltration is done with 15-30K membrane (note examples).
As regards claim 20 (interpreted as a pharmaceutical composition), Marquette teaches the nanoparticles are available for drug loading (e.g. drug delivery) of various antibodies (p.5-6, [0076]).
The motivation to produce a nano-assembly comprised within a nanoparticle is because of a need for polymer matrix-based nanoparticles comprising antibodies or other therapeutic, diagnostic or preventive proteins having: controlled release; and an increased encapsulation efficiency. The reference defines the materials and reagents with sufficient detail in order to make and use a nano-assembly complexed-nanoparticle with a reasonable degree of predictability and an assurance of success because of the limited number of reagents, the availability of the reagents, and the steps for producing the nano-assembly complexed-nanoparticle.
This rejection under 35 U.S.C. 103 might be overcome by: (1) a showing under 37 CFR 1.130(a) that the subject matter disclosed in the reference was obtained directly or indirectly from the inventor or a joint inventor of this application and is thus not prior art in accordance with 35 U.S.C.102(b)(2)(A); (2) a showing under 37 CFR 1.130(b) of a prior public disclosure under 35 U.S.C. 102(b)(2)(B); or (3) a statement pursuant to 35 U.S.C. 102(b)(2)(C) establishing that, not later than the effective filing date of the claimed invention, the subject matter disclosed and the claimed invention were either owned by the same person or subject to an obligation of assignment to the same person or subject to a joint research agreement. See generally MPEP § 717.02.
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.
13. Claims 1-14 and 20 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-10 of U.S. Patent No. 11957764.
The reference patent is not afforded safe harbor under 35 USC 121 because it shares no continuity nor a restriction/speciation with the claims of the instant application.
Although the claims at issue are not identical, they are not patentably distinct from each other because the claims share the common technical feature of a nano-assembly comprised within a nanoparticle, wherein the nano-assembly comprises a polyester and a protein comprising a hydrophobic domain, e.g., albumin, wherein the hydrophobic domain of the protein is bound with the polyester through hydrophobic interactions, wherein the protein further comprises a single chain antibody fragment with binding ability for an antigen that when combined with other proteins of the invention generates a multi-specific antibody forming a nano-assembly comprised within the nanoparticle. The reference patent claims anticipate and render obvious the scope of the instant claimed.
Ref claims
1. A multi-specific antibody delivery platform, which is formed by bonding a protein-type nanoparticle with an anti-Fc antibody through a chemical bond, wherein the protein-type nanoparticle includes polyester and a protein with a hydrophobic domain, and the hydrophobic domain of the protein is bound with the polyester through hydrophobic interaction, wherein the protein is albumin or a cell wall protein, and the protein has a same species as a recipient of the delivered specific antibody, wherein the anti-Fc antibody is an anti-IgG-Fc antibody; a weight ratio of the polyester to the protein is within a range of 1:(9-11); a Fab domain of the anti-Fc antibody is non-covalently bound with an Fc domain of a delivered specific antibody; and the delivered specific antibody has a same species as an Fc segment recognized by the anti-Fe antibody.
2. The multi-specific antibody delivery platform of claim 1, wherein the protein is at least one of a human serum albumin, a bovine serum albumin, a mouse serum albumin, an ovalbumin, a protein A, or protein G.
3. The multi-specific antibody delivery platform of claim 1, wherein the polyester is aliphatic polyester or polyethylene glycol-modified aliphatic polyester.
4. The multi-specific antibody delivery platform of claim 3, wherein the aliphatic polyester is at least one of polylactic acid, polyglycolide, poly(glycolide-co-lactide), or polycaprolactone; and the polyethylene glycol-modified aliphatic polyester is at least one of polyethylene glycol-modified polylactic acid, polyethylene glycol-modified polyglycolide, polyethylene glycol-modified poly(glycolide-co-lactide), or polyethylene glycol-modified polycaprolactone.
5. The multi-specific antibody delivery platform of claim 4, wherein the aliphatic polyester is polylactic acid; the polylactic acid is L-polylactic acid, D-polylactic acid, or racemic polylactic acid; and a terminal group of the polylactic acid is at least one of an ester group, a carboxyl group, or a hydroxyl group.
6. The multi-specific antibody delivery platform of claim 5, wherein the polylactic acid is the L-polylactic acid, a terminal group of the L-polylactic acid is the ester group, and a molecular weight of the L-polylactic acid is within a range of 7200 Daltons-1100000 Daltons.
7. The multi-specific antibody delivery platform of claim 4, wherein a ratio of LA/GA in the poly(glycolide-co-lactide) is within a range of 95/5-50/50.
8. The multi-specific antibody delivery platform of claim 1, wherein an average particle size of the protein-type nanoparticle is within a range of 100 nm to 200 nm.
9. The multi-specific antibody delivery platform of claim 1, wherein the multi-specific antibody delivery platform delivers at least two specific antibodies.
10. A mufti-specific antibody delivery system, comprising the multi-specific antibody delivery platform of claim 1 and a specific antibody.
14. Claims 1-14 and 20 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-19 of copending Application No. 18/363,747 (reference application US 20240083976). Although the claims at issue are not identical, they are not patentably distinct from each other because the claims share the common technical feature of a nano-assembly comprised within a nanoparticle, wherein the nano-assembly comprises a polyester and a protein comprising a hydrophobic domain, e.g., albumin, wherein the hydrophobic domain of the protein is bound with the polyester through hydrophobic interactions, wherein the protein further comprises a single chain antibody fragment with binding ability for an antigen that when combined with other proteins of the invention generates a multi-specific antibody forming a nano-assembly comprised within the nanoparticle. The reference claims anticipate and/or render obvious the scope of the instant claimed invention.
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This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Conclusion
15. No claims are allowed.
16. Any inquiry concerning this communication or earlier communications from the examiner should be directed to LYNN A. BRISTOL whose telephone number is (571)272-6883. The examiner can normally be reached Mon-Fri 9 AM-5 PM.
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/LYNN A BRISTOL/Primary Examiner, Art Unit 1643
Prosecution Insights