In vitro selection of a high affinity antibody to oestradiol using a phage display human antibody library

1996 ◽  
Vol 2 (3) ◽  
pp. 209-217 ◽  
Author(s):  
Anthony Pope ◽  
Kevin Pritchard ◽  
Andrew Williams ◽  
Andrew Roberts ◽  
John R. Hackett ◽  
...  
Keyword(s):  
Phage Display ◽  
In Vitro Selection ◽  
Human Antibody ◽  
Antibody Library ◽  
High Affinity ◽  
Selection Of

In vitro selection of high affinity HspR-binding sites within the genome of Helicobacter pylori

Gene ◽  
2002 ◽  
Vol 283 (1-2) ◽  
pp. 63-69 ◽  
Author(s):  
Isabel Delany ◽  
Gunther Spohn ◽  
Rino Rappuoli ◽  
Vincenzo Scarlato
Keyword(s):  
Helicobacter Pylori ◽  
Binding Sites ◽  
In Vitro Selection ◽  
High Affinity ◽  
Selection Of

In vitro selection of high-affinity nucleic acid ligands to parasite target molecules

2003 ◽  
Vol 33 (12) ◽  
pp. 1309-1317 ◽  
Author(s):  
H.Ulrich Göringer ◽  
Matthias Homann ◽  
Mihaela Lorger
Keyword(s):  
Nucleic Acid ◽  
In Vitro Selection ◽  
High Affinity ◽  
Target Molecules ◽  
Selection Of

scholarly journals A novel, stable, helical scaffold as an alternative binder - construction of phage display libraries.

2012 ◽  
Vol 59 (3) ◽  
Author(s):  
Anna Cyranka-Czaja ◽  
Jacek Otlewski
Keyword(s):  
Phage Display ◽  
Measles Virus ◽  
In Vitro Selection ◽  
Biophysical Properties ◽  
Phage Display Technology ◽  
High Affinity ◽  
Promising Tool ◽  
Phage Display Libraries ◽  
Display Technology

Specific, high affinity binding macromolecules are of great importance for biomedical and biotechnological applications. The most popular classical antibody-based molecules have recently been challenged by alternative scaffolds with desirable biophysical properties. Phage display technology applied to such scaffolds allows generation of potent affinity reagents by in vitro selection. Here, we report identification and characterization of a novel helical polypeptide with advantageous biophysical properties as a template for construction of phage display libraries. A three-helix bundle structure, based on Measles virus phosphoprotein P shows a very favourable stability and solubility profile. We designed, constructed and characterized six different types of phage display libraries based on the proposed template. Their functional size of over 10(9) independent clones, balanced codon bias and decent display level are key parameters attesting to the quality and utility of the libraries. The new libraries are a promising tool for isolation of high affinity binders based on a small helical scaffold which could become a convenient alternative to antibodies.

scholarly journals Antibody-like proteins that capture and neutralize SARS-CoV-2

2020 ◽  
Vol 6 (42) ◽  
pp. eabd3916 ◽  
Author(s):  
T. Kondo ◽  
Y. Iwatani ◽  
K. Matsuoka ◽  
T. Fujino ◽  
S. Umemoto ◽  
...  
Keyword(s):  
High Speed ◽  
In Vitro Selection ◽  
Nasal Swab ◽  
Inhibitory Concentration ◽  
Rapid Development ◽  
Spike Protein ◽  
Emerging Pathogens ◽  
High Affinity ◽  
Selection Of

To combat severe acute respiratory syndrome–related coronavirus 2 (SARS-CoV-2) and any unknown emerging pathogens in the future, the development of a rapid and effective method to generate high-affinity antibodies or antibody-like proteins is of critical importance. We here report high-speed in vitro selection of multiple high-affinity antibody-like proteins against various targets including the SARS-CoV-2 spike protein. The sequences of monobodies against the SARS-CoV-2 spike protein were successfully procured within only 4 days. Furthermore, the obtained monobody efficiently captured SARS-CoV-2 particles from the nasal swab samples of patients and exhibited a high neutralizing activity against SARS-CoV-2 infection (half-maximal inhibitory concentration, 0.5 nanomolar). High-speed in vitro selection of antibody-like proteins is a promising method for rapid development of a detection method for, and of a neutralizing protein against, a virus responsible for an ongoing, and possibly a future, pandemic.

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