Velappan et al., 2021 - Google Patents
Construction, characterization and crystal structure of a fluorescent single-chain Fv chimeraVelappan et al., 2021
View HTML- Document ID
- 1139117254391018314
- Author
- Velappan N
- Close D
- Hung L
- Naranjo L
- Hemez C
- DeVore N
- McCullough D
- Lillo A
- Waldo G
- Bradbury A
- Publication year
- Publication venue
- Protein Engineering, Design and Selection
External Links
Snippet
In vitro display technologies based on phage and yeast have a successful history of selecting single-chain variable fragment (scFv) antibodies against various targets. However, single-chain antibodies are often unstable and poorly expressed in Escherichia coli. Here …
- 102000005632 Single-Chain Antibodies 0 title abstract description 10
Classifications
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by the preceding groups
- G01N33/48—Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/53—Immunoassay; Biospecific binding assay
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/55—Fab or Fab'
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/10—Processes for the isolation, preparation or purification of DNA or RNA
- C12N15/1034—Isolating an individual clone by screening libraries
- C12N15/1037—Screening libraries presented on the surface of microorganisms, e.g. phage display, E. coli display
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/10—Processes for the isolation, preparation or purification of DNA or RNA
- C12N15/1034—Isolating an individual clone by screening libraries
- C12N15/1062—Isolating an individual clone by screening libraries mRNA-Display, e.g. polypeptide and encoding template are connected covalently
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/44—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material not provided for elsewhere, e.g. haptens, metals, DNA, RNA, amino acids
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/30—Immunoglobulins specific features characterized by aspects of specificity or valency
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/08—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from viruses
- C07K16/10—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from viruses from RNA viruses, e.g. hepatitis E virus
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/60—Immunoglobulins specific features characterized by non-natural combinations of immunoglobulin fragments
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
Similar Documents
Publication | Publication Date | Title |
---|---|---|
McMahon et al. | Yeast surface display platform for rapid discovery of conformationally selective nanobodies | |
Chen et al. | A cell-free nanobody engineering platform rapidly generates SARS-CoV-2 neutralizing nanobodies | |
Tereshko et al. | Toward chaperone‐assisted crystallography: protein engineering enhancement of crystal packing and X‐ray phasing capabilities of a camelid single‐domain antibody (VHH) scaffold | |
Sahtoe et al. | Reconfigurable asymmetric protein assemblies through implicit negative design | |
Braun et al. | Peptides in headlock–a novel high-affinity and versatile peptide-binding nanobody for proteomics and microscopy | |
Schmitz et al. | Structural evaluation of EGFR inhibition mechanisms for nanobodies/VHH domains | |
Sethi et al. | Differential epitope positioning within the germline antibody paratope enhances promiscuity in the primary immune response | |
McConnell et al. | An integrated approach to extreme thermostabilization and affinity maturation of an antibody | |
Correa et al. | Potent and specific inhibition of glycosidases by small artificial binding proteins (Affitins) | |
Millward et al. | In situ click chemistry: from small molecule discovery to synthetic antibodies | |
Sahtoe et al. | Transferrin receptor targeting by de novo sheet extension | |
Zhao et al. | Broadening a SARS-CoV-1–neutralizing antibody for potent SARS-CoV-2 neutralization through directed evolution | |
Bacon et al. | Screening yeast display libraries against magnetized yeast cell targets enables efficient isolation of membrane protein binders | |
Velappan et al. | Construction, characterization and crystal structure of a fluorescent single-chain Fv chimera | |
Sevy et al. | Structure-and sequence-based design of synthetic single-domain antibody libraries | |
Nannini et al. | Combining phage display with SMRTbell next-generation sequencing for the rapid discovery of functional scFv fragments | |
Steemson et al. | Tracking molecular recognition at the atomic level with a new protein scaffold based on the OB-fold | |
Kajiwara et al. | Development of a yeast cell surface display method using the SpyTag/SpyCatcher system | |
Weaver-Feldhaus et al. | Directed evolution for the development of conformation-specific affinity reagents using yeast display | |
Zeytun et al. | Fluorobodies combine GFP fluorescence with the binding characteristics of antibodies | |
Wang et al. | Development of a functional antibody by using a green fluorescent protein frame as the template | |
Senutovitch et al. | A variable light domain fluorogen activating protein homodimerizes to activate dimethylindole red | |
Taussig et al. | Development of proteome‐wide binding reagents for research and diagnostics | |
Krohl et al. | A suspension cell‐based interaction platform for interrogation of membrane proteins | |
Stains et al. | A general approach for receptor and antibody-targeted detection of native proteins utilizing split-luciferase reassembly |