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 .
DETAILED ACTION
Applicant’s election without traverse of Group I, claims 1-14 and 40, as well as the species: 1) PD-1 as the specific type I membrane protein; 2) 4-1BBL as the specific type II membrane protein, in the reply filed on September 12, 2025 is acknowledged.
Claims 15-34, 38, 41-45 and 47-50 were previously canceled.
Claims 1-14, 35-37, 39, 40, and 46 are pending.
Claims 35-37, 39 and 46 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to nonelected inventions or species, there being no allowable generic or linking claim.
Claims 1-14 and 40 are pending and under consideration.
Priority
It is acknowledged that this application is a 371 application of International Application: PCT/IL2020/050762, filed July 8, 2020, which claims the benefit of priority to U.S. Provisional Patent Appl. No. 62/872,741 filed July 11, 2019. The priority date has been established as: July, 11, 2019.
Information Disclosure Statement
The Information Disclosure Statements filed on 03/16/2022, 03/16/2022, 03/24/2022, 04/05/2022, 05/03/2022, 05/08/2022, 05/17/2022, 05/23/2022, 06/06/2022, 06/12/2022, 06/26/2022, 07/02/2022, 07/31/2022, 08/07/2022, 08/16/2022, 09/11/2022, 10/11/2022, 10/19/2022, 10/30/2022, 11/12/2022, 11/27/2022, 12/27/2022, 01/01/2023, 01/29/2023, 02/05/2023, 02/19/2023, 03/05/2023, 03/26/2023, 04/02/2023, 04/23/2023, 04/30/2023, 04/30/2023, 05/14/2023, 05/21/2023, 05/30/2023, 06/11/2023, 06/18/2023, 06/26/2023, 07/02/2023, 07/09/2023, 07/16/2023, 07/23/2023, 07/30/2023, 07/30/2023, 08/06/2023, 08/20/2023, 08/29/2023, 09/03/2023, 09/18/2023, 10/08/2023, 10/15/2023, 10/22/2023, 10/29/2023, 11/12/2023, 11/19/2023, 11/27/2023, 12/14/2023, 12/25/2023, 12/31/2023, 01/07/2024, 01/22/2024, 01/28/2024, 02/04/2024, 02/25/2024, 03/31/2024, 04/30/2024, 06/16/2024, 07/02/2024, 07/21/2024, 09/22/2024, 10/06/2024, 10/13/2024, 10/20/2024, 11/03/2024, 12/15/2024, 12/31/2024, 01/13/2025, 03/13/2025 have been considered and entered by examiner.
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.
Claim 40 is rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Claim 40 recites the limitation "encoding same" in line 2. There is insufficient antecedent basis for this limitation in the claim.
Claim 40 recites “a cell comprising same for…”. It is unclear what the term “same” refers to.
Claim 40 recite “system encoding”. It is unclear to one ordinary skill in the art what the term “system” encompasses, other than a nucleic acid encoding a protein/peptide.
Claim Rejections - 35 USC § 112
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Claims 1-14 and 40 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention. This is a WRITTEN DESCRIPTION rejection.
Claim 1 is drawn to “a heterodimer comprising a dimerizing moiety attached to at least one amino acid sequence of at least one type I membrane protein capable of at least binding a natural ligand or receptor of said at least one type I membrane protein and to at least one amino acid sequence of at least one type II membrane protein capable of at least binding a natural ligand or receptor of said at least one type II membrane protein”. Given Broadest Reasonable Interpretation (BRI), the claim would encompass:
A broad genus of dimerizing moiety. Based on paragraphs [0123] – [0126] of the instant publication US 2022/0267409 A1, the dimerizing can be non-proteinaceous moiety, e.g. a cross linker, an organic polymer, a synthetic polymer, a small molecule and the like ([0123]), or the dimerizing moiety can be a proteinaceous moiety comprises members of affinity pairs ([0125]). These dimerizing moieties vary significantly, have different structures, different physical and chemical properties, and have different mechanism to form dimers.
A broad genus of type I membrane proteins.
A broad genus of Type II membrane proteins.
As evidenced by Fromm (Fromm et al., Journal for ImmunoTherapy of Cancer, (2018) 6: 149, Publication Year: 12/18/2018), in human genome there are >1400 type I and >450 type II single-pass membrane protein encoding genes. Thus, just considering one plus one combinations, there are more than half million possible type I/type II membrane protein combinations. Taking account of unlimited dimerizing moieties, the number of combinations for dimerizing moiety/type I/type II membrane proteins are even bigger.
In addition, the claim and specification do not limit the term “attached”. Given BRI, the dimerizing moiety can be directly or indirectly attached to the amino acid sequence of type I or type II membrane protein; can be covalently or non-covalently attached to the amino acid sequence of type I or type II membrane protein; can be attached via bonding at the carboxy/amino termini of the amino acid sequence of type I or type II membrane protein or via bonding to internal chemical groups straight, branched or cyclic side chains, internal carbon or nitrogen atoms.
Taken together, claim 1 encompasses a broad genus of heterodimers which vary significantly; have different structures, different physical and chemical properties; and have different mechanism to form dimers. However, the specification lacks written description support for the broadly claimed genera.
The written description requirement for a claimed genus may be satisfied through sufficient description of a representative number of species by actual reduction to practice, reduction to drawings, or by disclosure of relevant, identifying characteristics, i.e., structure or other physical and/or chemical properties, by functional characteristics coupled with a known or disclosed correlation between function and structure, or by a combination of such identifying characteristics, sufficient to show the applicant was in possession of the claimed genus. (See Federal Register, Vol. 66, No. 4, pages 1099-1111, Friday January 5, 2001, especially page 1106 3rd column). A "representative number of species" means that the species which are adequately described are representative of the entire genus. Thus, when there is substantial variation within the genus, one must describe a sufficient variety of species to reflect the variation within the genus. MPEP 2163 II.A.3a.ii.
Regarding the claimed dimerizing moieties, it is well known in the art, for synthetic multiprotein complex, structural flexibility is essential to facilitate the various activities and is often affected by the changes in secondary, tertiary and quaternary structure of proteins. Typically, at the residue level the bond length, bond rotation and rotation angle are vital in bringing notable conformational changes, as evidence by the first paragraph of introduction of Patel (Patel et al., Protein Expression and Purification 191 (2022) 106012). Different dimerizing moieties vary significantly in size, for example a Fc domain has a molecular weight about 26 kDa, but LC-SMCC (a non-proteinaceous dimerizing moiety, see paragraph [0124] of the instant publication US 2022/0267409 A1) has a molecular weight of 447.5. In addition, Fc domain and LC-SMCC have different mechanisms to be linked with an amino acid sequences. Therefore, the heterodimer made with different dimerizing moieties (e.g. PD-1-Fc-4-1BBL vs PD-1-LC-SMCC-4-1BBL) would have different secondary, tertiary and/or quaternary structure. Other than general description (paragraphs [0123] – [0126] of the instant publication US 2022/0267409 A1), the specification disclose heterodimers comprising only one specific dimerizing moiety: Fc domain, see Example 1, [0857]-[0869]). It is well known that compared to other dimerizing moieties, the Fc domain has some specific functions, e.g. binds to Fc receptors on immune cells. Thus, the heterodimers comprising a Fc domain would have different therapeutic properties compared with heterodimers comprising other dimerizing moieties. Taken together, the specification have not provided a sufficient description about the correlation between the function (e.g. binding natural ligands or receptors, and/or therapeutic activity) and the structure of the heterodimer (e.g. the structure of dimerizing moiety) and one of ordinary skilled in the art would not be able to readily recognize/visualize which heterodimers with a dimerizing moiety (other than the Fc domain) would have the required properties and functions (e.g. treating disease).
Regarding claimed type I membrane proteins and type II membrane proteins, the specification discloses a number of type I and type II membrane proteins, as evidenced by claims 5 and 8. The specification disclose a few heterodimers, including DSP305, DSP305-V1, TSP111, TSP111_V1, TSP111_V2, TSP112, DSP214, DSP214_v1, TSP215, TSP215_v1, TSP217, DSP218, TSP221, TSP222, TSP401, TSP403, TSP501 and TSP503 (see [0876]). Only five type I membrane proteins (PD1 (the elected species), SIRPα, LILRB2, SIGLEC10, TIGIT) and two type II membrane proteins (4-1BBL (the elected species), CD40L) have been disclosed in Examples (see [0876]). As set forth above, the scope of the claim is not limited to the type I and type II membrane proteins recited by claims 5 and 8. As evidenced by Table 1 and Table 2 of Schreiber et al. (pages 41-123, US 2019/0151413 A1, cited as No.17 reference in IDS of 03/16/2022), a large number of type I membrane proteins and type II proteins combinations are encompassed by the instant claim. The type I and type II membrane proteins have different functions, for example PD-1 inhibits T-cell activity but Toll-like receptors (TLRs) (which are also type I membrane protein, see page 84 of Schreiber) trigger immune and inflammatory responses. Taken together, the specification have not provided a sufficient description about the correlation between the function (e.g. therapeutic activity) and the structure of the heterodimer (e.g. the combination of type I and type II membrane proteins) and one of ordinary skilled in the art would not be able to readily recognize/visualize which heterodimers with a dimerizing moiety (other than the combinations disclosed by the examples of the instant specification) would have the required properties and functions (e.g. treating disease).
In addition, given BRI, the dimerizing moiety can be attached via bonding at the amino/carboxy termini of the amino acid sequence of type I or type II membrane protein or via bonding to internal chemical groups straight, branched or cyclic side chains, internal carbon or nitrogen atoms. However, all of the heterodimers have amino acid sequence(s) type I membrane protein fused at the N-term of the Fc domain and amino acid sequence(s) of type II membrane protein fused at the C-term of the Fc domain. No other format is disclosed by the specification (see Example 1, [0857]-[0869]). Heterodimers with different format would have different structures (including tertiary and quaternary structure) and physical/chemical properties. One of ordinary skilled in the art would not be able to readily recognize/visualize other “attaching formats” would be functional equivalent to the only format used in the examples.
In addition, as evidenced by claim 3, claim 1 encompasses heterodimers wherein the monomers of said heterodimer are covalently attached and non-covalently attached. However, all heterodimers disclosed in the specification comprise Fc domains with the hinge cysteine residues which stabilize the complex, see [0080], [0082], [0084], [0086] and [0088] of the instant publication US 2022/0267409 A1. It is well known in the art that the hinge cysteine residues forms bisulfide bond (a covalent bond) between two Fc domains (monomers). The specification does not disclose any heterodimer wherein the monomers are non-covalently attached to each other.
The Examiner acknowledges that a working example or exemplified embodiment is not necessarily a requirement for description. However, where a generic claim term is present in a claim, as in the present application, and defined only by functional characteristics, the specification must convey enough information, e.g., via sufficient representative examples, to indicate invention of species sufficient to constitute the genus. Enzo Biochem, Inc. v. Gen-Probe Inc., 323 F.3d 956, 967 2 (Fed. Cir. 2002). The written description requirement “requires a description of an invention, not an indication of a result that one might achieve if one made that invention.” Regents of the University of California v. Eli Lilly & Co., 119 F.3d 1559, 1568 (Fed. Cir. 1997); see also Novozymes A/S v. DuPont Nutrition Biosciences APS, 723 F.3d 1336, 1350 (Fed. Cir. 2013) (“A patent...‘is not a reward for the search, but compensation for its successful conclusion.’ ... For that reason, the written description requirement prohibits a patentee from ‘leaving it to the ... industry to complete an unfinished invention.’” (citations omitted)).
Claims 2-14 and 40 also encompass 1) a broad genus of dimerizing moieties; 2) a broad genus of type I membrane proteins; and/or 3) a broad genus of type II membrane proteins. Accordingly, the specification lacks adequate written description for claims 1-14 and 40.
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 pre-AIA 35 U.S.C. 103(a) which forms the basis for all obviousness rejections set forth in this Office action:
(a) A patent may not be obtained though the invention is not identically disclosed or described as set forth in section 102, if the differences between the subject matter sought to be patented and the prior art are such that the subject matter as a whole would have been obvious at the time the invention was made to a person having ordinary skill in the art to which said subject matter 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 pre-AIA 35 U.S.C. 103(a) 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.
This application currently names joint inventors. In considering patentability of the claims under pre-AIA 35 U.S.C. 103(a), the examiner presumes that the subject matter of the various claims was commonly owned at the time any inventions covered therein were made absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and invention dates of each claim that was not commonly owned at the time a later invention was made in order for the examiner to consider the applicability of pre-AIA 35 U.S.C. 103(c) and potential pre-AIA 35 U.S.C. 102(e), (f) or (g) prior art under pre-AIA 35 U.S.C. 103(a).
Claims 1, 2, 4-14 and 40 are rejected under pre-AIA 35 U.S.C. 103(a) as being unpatentable over Schreiber (Schreiber et al., US 2019/0151413 A1, Publication Date: 05/23/2019, cited as No. 17 reference in IDS of 03/16/2022), in view of Sturgill (Sturgill et al., AJHO. 2017; 13(11): 4-15, Publication Year: 2017) and Ha (Ha et al., Frontiers in Immunology, vol. 7, article 394, Publication Date: 10/06/2016).
Schreiber teaches a fusion protein comprising: (a) a first extracellular domain of type I transmembrane protein at the N-terminus, (b) a second extracellular domain of a type II transmembrane protein at the C-terminus, (c) a linker ([0005], [0012], and Fig. 1).
Schreiber teaches that in some embodiments, the fusion protein comprises the extracellular domain of PD-1 and is paired with ab immune stimulatory agent such as: PD1/4-1BBL, PD-1/OX-40L, PD-1/LIGHT, PD-1/GITRL, PD-1/CD30L, PD-1/CD-40L ([0053]). Schreiber teaches making various fusion proteins including CD172a-Fc-OX40L, TIGIT-Fc-OX40L, PD-1-FC-GITRL, PD-1-Fc-41BBL, PD1-Fc-TL1A, CD172a-Fc-CD40L (see Fig. 17A, Example 5).
Schreiber teaches that in various embodiments, the linker comprises an Fc domain of an antibody, such as a hinge-CH2-Ch3 Fc domain derived from IgG4 or IgG1 ([0097]). Schreiber teaches that there are dimeric formation for the fusion protein ([0205]). As evidenced by the instant claim 4, Fc domain is a dimerizing moiety.
Schreiber teaches that the Fc domain linker may contain one or more mutations ([0098]-[0101]).
Schreiber teaches that the linker may function to improve the folding and/or stability, or improve the pharmacokinetics ([0105]).
Schreiber teaches that the fusion proteins can be co-administered ([0141]).
Schreiber teaches the method of making PD-1-Fc-OX40L protein (Example 1). Binding assays showed that PD-1-Fc-OX40L can bind OX40 and PD-L1. Thus, the amino acid sequence of type I membrane protein or type II membrane protein is capable of binding a natural ligand ([0202]).
Schreiber teaches that in vivo administration of PD-1-Fc-OX40L led to tumor regression in the B16.F10-ova tumor model ([0204]). Schreiber teaches that the PD-1-Fc-4-1BBL and PD-1-Fc-GITRL also led to reduced tumor size in treated animals ([0208])
Schreiber teaches that administration of PD-1-Fc-OX40L, PD1-Fc-GITRL, and CD172a-Fc-CD40L all led to reduced tumor growth in mice bearing MC38 tumors ([0210] and Fig 11E). It is noted that CD172a is also called SIRPa, as evidenced by claim 73 of Schreiber.
Schreiber teaches that PD-1-Fc-OX40L resulted in greater tumor regression that the OX40 agonist and PD-L1 blocking antibody in CT26 colorectal cancer model (Fig. 11L and [0212]).
Schreiber teaches treating cancers with the pharmaceutical composition comprising the fusion protein (claim 71).
Schreiber’s teachings are described above. However, Schreiber does not explicitly teach a heterodimer comprising the recited components.
Sturgill teaches that the tumor microenvironment is often immunosuppressive and lacks the appropriate signals necessary for stimulating effective anti-tumor T-cell responses (Abstract).
Sturgill teaches that T cells express both activating (such as 4-1BB and OX40) and inhibitory receptors (such as PD-1). These receptors can be targeted in order to increase T-cell activation (see Figure on page 6).
Sturgill teaches that 4-1BB agonist in combination with OX40 agonist and PD-1 inhibitor combination has been tested in clinical settings (page 7, col. 2, para. 2).
Ha teaches that use heterodimeric Fc as alternative scaffold of wild-type Fc for naturally heterodimeric proteins, to create Fc-fusion proteins with novel therapeutic modality (Abstract).
Ha teaches methods making heterodimeric Fc variant: “Knobs-into-Hole (KiH)” Fc technology (page 3, col. 1, para. 1; and Fig. 2B).
Ha teaches that heterodimeric Fc technology is now emerging as a promising scaffold for the generation of Fc-fused protein. The heterodimeric Fc capability will facilitate the development of the next generation of Fc-fused proteins that maintain full function of the fusion partner, while retaining the Fc-mediated extended half-life and immune effector functions (the bridging paragraph of cols. 1-2 on page 13).
It would have prima facie been obvious to one of ordinarily skilled in the art at the time the invention was filed to make various Fc fusion proteins such as PD-1-Fc-OX40L, PD-1-Fc-4-1BBL and PD-1-Fc-GITRL for treating cancers as taught by Schreiber, and to combine the Fc fusion proteins e.g. PD-1-Fc-OX40L+ PD-1-Fc-4-1BBL, because Schreiber teaches that both fusion proteins are effective in reducing B16.F10-ova tumor. Schreiber also teaches that the fusion proteins can be used in combination. Sturgill teaches that targeting PD-1, OX40 and 4-1BBL can increase T cell activation. One of ordinary skill in the art would further modify the fusion protein by using a heterodimeric Fc as alternative scaffold to bring the two fusion protein together, because Ha teaches that heterodimeric Fc (such as KiH) is widely used in the art, can create Fc-fusion proteins with novel therapeutic modality, and the heterodimeric Fc format can maintain full function of the fusion partner, while retaining the Fc-mediated extended half-life and immune effector functions. Based on the teachings of the references, one of ordinary skill in the art would have had a reasonable expectation that the heterodimer of PD-1-Fc-OX40L and PD-1-Fc-4-1BBL would have enhanced therapeutic activity to cancers (such as ovary cancer) because both monomers have anti-tumor activity in B16.F10-ova tumor model. The motivation would be to develop a more potent therapeutic composition for treating cancers.
Regarding claim 11, as evidenced by Sturgill, both PD1 and 4-1BBL are immune modulators, because they regulate T cell activation (see Figure on page 6).
Regarding claims 12 and 13, a heterodimer comprising PD-1-Fc-OX40L and PD-1-Fc-4-1BBL would read on the claims, because both monomers comprise one amino acid sequence of at least one type I membrane protein and one amino acid sequence of at least one type II membrane protein.
Regarding claim 14, the monomer PD-1-Fc-OX40L would read on the limitation “a first monomer comprising at least one of said at least two amino acid sequences of said at least two type I membrane proteins and said at least one amino acid sequence of said at least one type II membrane protein”; and the monomer PD-1-Fc-4-1BBL would read on the limitation: “a second monomer comprising at least one of said at least two amino acid sequences of said at least two type I membrane proteins”.
Claim 3 is rejected under pre-AIA 35 U.S.C. 103(a) as being unpatentable over Schreiber (Schreiber et al., US 2019/0151413 A1, Publication Date: 05/23/2019, cited as No. 17 reference in IDS of 03/16/2022), in view of Sturgill (Sturgill et al., AJHO. 2017; 13(11): 4-15, Publication Year: 2017) and Ha (Ha et al., Frontiers in Immunology, vol. 7, article 394, Publication Date: 10/06/2016), as applied to claims 1, 2, 4-14 and 40, and further in view of Yang (Yang et al., Frontiers in Immunology, Vol. 8, Article 1860, Publication Date: 01/08/2018).
Schreiber, Sturgill and Ha teach the heterodimer of claim 1 as set forth above. However, Schreiber, Sturgill and Ha don’t teach wherein monomers of said heterodimer are not covalently attached.
Yang teaches that the covalent interactions are typically caused by the formation of disulfide bonds between two cysteine residues; and the non-covalent interactions include hydrogen bonds, Van der Waals forces, hydrophobic interactions, and salt bridges (page 3, col. 2, para. 2).
Yang teaches that Fc domains have both covalent interactions (page 5, col. 1, para. 3) and non-covalent interactions (§ Optimization on Non-Covalent Interaction in Fc).
Yang teaches that although disulfide bonds can increase the stability of a protein, the risk of increasing aggregation propensity might not be neglected (page 6, col. 2, para. 2).
Yang teaches introduction of intermolecular non-covalent interactions in CH3 (the bridging paragraph of pages 7-8, and Table 1).
Yang teaches that optimization of non-covalent interaction can lead to a better Fc with more stable, more aggregation-resistant and more soluble characteristics (page 8, col. 1, para. 2).
It would have prima facie been obvious to one of ordinarily skilled in the art at the time the invention was filed to make a heterodimer of the claim 1 (e.g. PD-1-Fc-OX40L and PD-1-Fc-4-1BBL heterodimer) based on the teachings of Schreiber, Sturgill and Ha, as set forth above, and to further modify the Fc domain based on the teachings of Yang by removing the covalent interaction between Fc domain (removing disulfide bond) and optimizing non-covalent interaction of Fc domain, because Yang teaches that disulfide bonds can increase aggregation, and optimization of non-covalent interaction can lead to a better Fc with more stable, more aggregation-resistant and more soluble characteristics. Yang also teaches possible mutations in the CH3 regions. Given that the method of making the mutations are well known in the art, as evidenced by Yang, one of ordinary skill in the art would have had a reasonable expectation of success to making the heterodimer wherein monomers are not covalently attached, and one of ordinary skill in the art would have had a reasonable expectation that the heterodimer wherein the monomers with optimized non-covalent interaction (not covalently attached) would have had better properties such as more stable, more aggregation-resistant and more soluble, as Yang recognized. The motivation would have been to expand the varieties of the heterodimers and to develop a heterodimers with better pharmaceutical properties.
Conclusion
No claims are allowed.
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/CHENG LU/ Examiner, Art Unit 1642