# US 10,870,926 B2 · Antibody like protein

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- Number: US 10,870,926 B2
- Document ID: US10870926B2
- Status: Granted
- Kind: B2
- Application number: 16/445,121
- Filed: 2019-06-18
- Published: 2019-10-17
- Granted: 2020-12-22
- Earliest claimed: 2013-09-25
- Assignees: Idea Orchard, LLC
- Applicants: Idea Orchard, LLC
- Inventors: Michael Longo; Rajika Perera
- Web page: https://patentgrep.com/patent/US10870926B2

## CPC

- C07K 14/4702: {Regulators; Modulating activity}
- C40B 40/10: Libraries containing peptides or polypeptides, or derivatives thereof
- C12N 9/90: Isomerases (5.)
- C12N 15/102: {Mutagenizing nucleic acids}
- C12N 15/1031: {mutagenesis by gene assembly, e.g. assembly by oligonucleotide extension PCR}
- C12N 15/1037: {Screening libraries presented on the surface of microorganisms, e.g. phage display, E. coli display}
- C40B 10/00: Directed molecular evolution of macromolecules, e.g. RNA, DNA or proteins
- C40B 40/08: Libraries containing RNA or DNA which encodes proteins, e.g. gene libraries
- C07K 2319/00: Fusion polypeptide
- C07K 2319/20: containing a tag with affinity for a non-protein ligand
- C07K 2319/50: containing protease site
- C07K 2319/70: containing domain for protein-protein interaction
- C12N 15/1034: {Isolating an individual clone by screening libraries}
- C12N 15/1058: {Directional evolution of libraries, e.g. evolution of libraries is achieved by mutagenesis and screening or selection of mixed population of organisms}
- C07K: PEPTIDES (peptides in foodstuffs A23; obtaining protein compositions for foodstuffs, working-up proteins for foodstuffs A23J; preparations for medicinal purposes A61K; peptides containing beta-lactam rings C07D; cyclic dipeptides not having in their molecule any other peptide link than those which form their ring, e.g. piperazine-2,5-diones, C07D; ergot alkaloids of the cyclic peptide type C07D519/02; macromolecular compounds having statistically distributed amino acid units in their molecules, i.e. when the preparation does not provide for a specific; but for a random sequence of the amino acid units, homopolyamides and block copolyamides derived from amino acids C08G69/00; macromolecular products derived from proteins C08H1/00; preparation of glue or gelatine C09H; single cell proteins, enzymes C12N; genetic engineering processes for obtaining peptides C12N15/00; compositions for measuring or testing processes involving enzymes C12Q; investigation or analysis of biological material G01N33/00)
- C40B: COMBINATORIAL CHEMISTRY; LIBRARIES, e.g. CHEMICAL LIBRARIES (in silico combinatorial libraries of nucleic acids, proteins or peptides G16B35/00; in silico combinatorial chemistry G16C20/60)
- C12N: MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA (microbiological testing media C12Q1/00)

## Abstract

A general method and recombinant nucleic acid sequences, by means which the method selects a recombinant protein containing an FHA domain for binding a target molecule from a library proteins with a high-throughput method of creating protein variations within the FHA domain in non-conserved or non-structural sequences of the FHA scaffold, and the library may also be in the form of a phagemid or phage library wherein the ALP nucleic acid sequence is inserted into a vector capable of allowing the vector and expressed ALP protein from being virally packaged, and the recombinant nucleic acid sequences which are randomly mutated at varying non-conserved or non-structural FHA domain sequences.

## Claims

### Claim 1

A protein comprising:
a) a first FHA domain derived from a wild-type FHA domain wherein the first FHA domain comprises at least one mutation;
b) a multimer domain fused to the first FHA domain wherein the multimer domain is capable of forming multimeric proteins with at least one separately expressed protein;
c) a second FHA domain wherein the second FHA domain is a wild-type domain or has at least one mutation, and the second FHA domain is covalently attached to the first FHA domain; and
d) wherein the at least one mutation results in at least one of the FHA domains having specific binding affinity to a target molecule that includes interactions with non-naturally occurring FHA domain recognition sites.

### Claim 2 (depends on 1)

The protein of claim 1 wherein the multimer domain comprises a CC1 domain.

### Claim 3 (depends on 1)

The protein of claim 1 wherein the multimer domain comprises a fragment crystallizable region (Fc region).

### Claim 4

A protein comprising:
a) a first FHA domain derived from a wild-type FHA domain wherein the first FHA domain comprises at least one mutation;
b) a CC1 domain fused to the first FHA domain wherein the CC1 domain is capable of forming multimeric proteins with at least one separately expressed protein; and
c) a second FHA domain wherein the second FHA domain is a wild-type domain or has at least one mutation, and the second FHA domain is covalently attached to the first FHA domain.