Prior art

As a technical patent analyst, I have identified the most relevant prior art for US patent 12297278, "Wnt surrogate molecules and uses thereof," based on the provided patent text. The priority date of US12297278 is December 19, 2017.

The claims of US12297278 generally encompass soluble, bivalent, bispecific Wnt surrogate molecules comprising one or more Frizzled (Fzd) receptor binding regions and one or more Low-density lipoprotein (LDL) receptor-related protein 5 (LRP5) and/or LRP6 binding regions. These binding regions can be various antibody fragments (e.g., IgG, scFv, Fab, VHH, sdAb), may have specific CDR sequences or sequence identities, exhibit particular Fzd binding specificities, and can be arranged in various structural formats (e.g., Fab-IgG fusions, VHH/sdAb-Fc fusions, diabodies, FIT-IG formats). The patent also claims methods of modulating Wnt signaling and treating related diseases.

Below are the patent citations mentioned within the provided text of US12297278, along with their details and potential for anticipation under 35 U.S.C. § 102:

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1. U.S. Provisional Application No. 62/607,877

• Full Citation: U.S. Provisional Patent Application No. 62/607,877, titled "Anti-Frizzled Antibodies and Methods of Use."
• Publication/Filing Date: Filed on December 19, 2017.
• Brief Description: This provisional application describes anti-Frizzled antibodies and antigen-binding fragments thereof, along with methods for their use. The Fzd binding regions disclosed in this provisional are explicitly stated in US12297278 to be used as components of the Wnt surrogate molecules. [cite: the provided patent text]
• Potential Anticipation under 35 U.S.C. § 102: As US12297278 claims priority to this provisional application (indicated by the shared priority date and explicit incorporation by reference), this provisional primarily establishes the earliest effective filing date for the Fzd binding regions and associated methods described within. If any claims in US12297278 pertain solely to Fzd binding regions (e.g., specific Fzd antibodies, their CDR sequences, or their individual binding properties) and extend beyond the scope of disclosure of this provisional, or if the priority claim were found to be invalid for specific subject matter, then this provisional could potentially anticipate such claims.

2. U.S. Provisional Application No. 62/607,879

• Full Citation: U.S. Provisional Patent Application No. 62/607,879, titled "Anti-LRP5/6 Antibodies and Methods of Use."
• Publication/Filing Date: Filed on December 19, 2017.
• Brief Description: This provisional application describes anti-LRP5/6 antibodies and antigen-binding fragments thereof, and methods of their use. These LRP5/6 binding regions are explicitly mentioned in US12297278 as components of the Wnt surrogate molecules. [cite: the provided patent text]
• Potential Anticipation under 35 U.S.C. § 102: Similar to the above, this provisional primarily establishes the priority date for the LRP5/6 binding regions and related methods disclosed within. Should any claims in US12297278 relate exclusively to LRP5/6 binding regions (e.g., specific LRP5/6 antibodies, their CDR sequences, or their individual binding properties) and be found to contain subject matter not fully disclosed or enabled in this provisional, then this provisional could potentially anticipate those specific claims. Furthermore, if the combination of Fzd and LRP5/6 binding regions for Wnt agonism was sufficiently disclosed in these provisional applications (individually or combined), they could potentially anticipate broader claims regarding the bispecific Wnt surrogate molecule.

3. WO94/13804

• Full Citation: WO 1994/013804 A1 (Holliger et al.), "Multivalent or Multispecific Fragments of Antibodies constructed by gene fusion."
• Publication/Filing Date: International Filing Date: December 23, 1993; Publication Date: July 7, 1994.
• Brief Description: This PCT application describes "diabodies" as multivalent or multispecific antibody fragments created through gene fusion. It details how two polypeptide chains, each with VH and VL domains, can be engineered with short linkers to form inter-chain antigen-binding sites, and also mentions their selection via phage display. [cite: the provided patent text, 9]
• Potential Anticipation under 35 U.S.C. § 102: This document predates the priority date of US12297278 and serves as prior art for claims that define the Wnt surrogate molecule generally as a diabody or describe methods of constructing such molecules via gene fusion, particularly if these claims do not introduce novel structural modifications or unexpected functional benefits specific to the Wnt surrogate context beyond the general principles of diabody design.

4. U.S. Pat. No. 5,091,513

• Full Citation: U.S. Patent 5,091,513 (Huston et al.), "Polypeptide linkers for recombinant proteins."
• Publication/Filing Date: Filing Date: January 18, 1990; Publication Date: February 25, 1992.
• Brief Description: This patent discloses single-chain antigen-binding proteins (scFv) and methods for their production, with a focus on polypeptide linkers designed to connect the variable heavy and light chain domains to form functional scFv molecules. [cite: the provided patent text, 9]
• Potential Anticipation under 35 U.S.C. § 102: This patent is prior art for claims in US12297278 concerning the fundamental concept and construction of single-chain Fv (scFv) antibodies, including the use and design of polypeptide linkers. It could anticipate claims describing the Wnt surrogate molecule as comprising scFv fragments, where the scFv technology itself (e.g., its basic structure or linkage) is not claimed with specific novel improvements relevant to the Wnt surrogate function.

5. U.S. Pat. No. 5,132,405

• Full Citation: U.S. Patent 5,132,405 (Huston et al.), "Recombinant single-chain antigen-binding proteins."
• Publication/Filing Date: Filing Date: February 25, 1992; Publication Date: July 21, 1992.
• Brief Description: This patent, related to US 5,091,513, further details recombinant single-chain antigen-binding proteins (scFv) and their methods of expression and use, emphasizing their ability to retain antigen recognition and binding capabilities. [cite: the provided patent text, 9]
• Potential Anticipation under 35 U.S.C. § 102: Similar to US 5,091,513, this patent is prior art for claims in US12297278 that broadly cover scFv antibodies as antigen-binding fragments, their recombinant production, and their general functional properties, where the specific arrangement or therapeutic application within the Wnt surrogate context is not sufficiently distinguishing.

6. U.S. Pat. No. 4,946,778

• Full Citation: U.S. Patent 4,946,778 (Ladner et al.), "Single polypeptide chain binding molecules."
• Publication/Filing Date: Filing Date: January 20, 1989; Publication Date: August 7, 1990.
• Brief Description: This patent describes the construction and expression of single polypeptide chain binding molecules, including those with antigen-binding specificity, designed to mimic the binding ability of antibody variable regions.
• Potential Anticipation under 35 U.S.C. § 102: This patent is prior art for claims in US12297278 related to the foundational concept of creating single-chain antibody-mimetic binding molecules through genetic engineering. It could anticipate claims generally defining Wnt surrogate molecules as comprising single-chain antibody fragments or similar single polypeptides that bind to a target, where the innovation is not in the single-chain nature itself.

7. US20090226421

• Full Citation: U.S. Patent Application Publication 2009/0226421 A1 (van der Winkel et al.), "Hinge-modified antibodies."
• Publication/Filing Date: Filing Date: February 27, 2009; Publication Date: September 10, 2009.
• Brief Description: This publication describes hinge-modified IgG4 antibodies, specifically those with a removed hinge region, marketed as UniBody®. These modified antibodies are stable, smaller, and bind univalently, which can reduce interactions with the immune system.
• Potential Anticipation under 35 U.S.C. § 102: This publication predates the priority date of US12297278 and is prior art for claims that specifically utilize or describe hinge-modified IgG4 antibodies or the UniBody® format as a structural component for the Wnt surrogate molecules, particularly concerning the features of reduced size, univalent binding, and altered immune effector function. [cite: the provided patent text, 17]

8. U.S. Pat. No. 6,765,087

• Full Citation: U.S. Patent 6,765,087 (Muyldermans et al.), "Production of antibodies or (functionalized) fragments thereof derived from heavy chain immunoglobulins of camelidae."
• Publication/Filing Date: Filing Date: August 14, 2000; Publication Date: July 20, 2004.
• Brief Description: This patent describes methods for producing antibodies or fragments, specifically VHH or single-domain antibodies (sdAb), derived from heavy chain-only immunoglobulins found in camelids. It also covers their efficient production in various host organisms, such as E. coli. [cite: the provided patent text, 5]
• Potential Anticipation under 35 U.S.C. § 102: This patent is prior art for claims in US12297278 that broadly describe the use or production of VHH or sdAb (nanobody®) antibody fragments within the Wnt surrogate molecule, particularly regarding their single-domain nature and methods of recombinant production in prokaryotic or eukaryotic hosts.

9. U.S. Pat. No. 6,838,254

• Full Citation: U.S. Patent 6,838,254 B1 (Muyldermans et al.), "Production of antibodies or (functionalized) fragments thereof derived from heavy chain immunoglobulins of camelidae."
• Publication/Filing Date: Filing Date: August 11, 2004; Publication Date: January 4, 2005.
• Brief Description: This patent further details processes for producing antibodies or functionalized fragments (VHH/sdAb) derived from camelid heavy chain immunoglobulins, emphasizing their production in lower eukaryotic hosts like molds or yeast.
• Potential Anticipation under 35 U.S.C. § 102: This patent is prior art for claims in US12297278 relating to the production of VHH or sdAb fragments, specifically when produced in various host systems (e.g., molds, yeast). It could anticipate claims that describe Wnt surrogate molecules incorporating such VHH/sdAb components, particularly concerning their manufacturing methods.

10. PCT Application Publication No. WO2017/136820

• Full Citation: WO 2017/136820 A1 (Gong et al.), "FABS-IN-TANDEM IMMUNOGLOBULIN (FIT-IG)."
• Publication/Filing Date: International Filing Date: February 6, 2017; Publication Date: August 10, 2017.
• Brief Description: This PCT application describes "Fabs-in-tandem IgG (FIT-IG)" formats, which allow the combination of functions from two antibodies into a single molecule by rearranging DNA sequences of parental monoclonal antibodies. It highlights that FIT-IGs can form tetravalent bispecific antibodies without Fc mutations, scFv elements, or linkers. [cite: the provided patent text, 5]
• Potential Anticipation under 35 U.S.C. § 102: This publication, preceding the priority date of US12297278, is highly relevant prior art for any claims in US12297278 that describe Wnt surrogate molecules structured in a FIT-IG format. It anticipates claims defining the Wnt surrogate molecule as having a FIT-IG structure, especially where the claimed innovation does not go beyond the known architectural advantages or functional outcomes of the FIT-IG platform.

11. U.S. Pat. No. 8,507,442

• Full Citation: U.S. Patent 8,507,442 B2 (Gong et al.), "Frizzled binding agents and methods of use thereof."
• Publication/Filing Date: Filing Date: November 1, 2011; Publication Date: August 13, 2013.
• Brief Description: This patent describes frizzled binding agents, specifically anti-Frizzled antibodies, including OMP-18R5 (vantictumab), a pan-specific frizzled antibody. It provides the CDR sequences for OMP-18R5.
• Potential Anticipation under 35 U.S.C. § 102: This patent is prior art for claims in US12297278 that recite a Fzd binding domain comprising the six CDR regions of OMP-18R5 (vantictumab) or an scFv derived from it. Any claims in US12297278 that incorporate these specific, known Fzd binding sequences or their inherent binding properties without novel structural or functional modifications in the context of the bispecific Wnt surrogate molecule would be anticipated. [cite: the provided patent text]