Search results
Results from the WOW.Com Content Network
Antibody phage display was later used by Carlos F. Barbas at The Scripps Research Institute to create synthetic human antibody libraries, a principle first patented in 1990 by Breitling and coworkers (Patent CA 2035384), thereby allowing human antibodies to be created in vitro from synthetic diversity elements.
In immunology, affinity maturation is the process by which T FH cell-activated B cells produce antibodies with increased affinity for antigen during the course of an immune response. With repeated exposures to the same antigen, a host will produce antibodies of successively greater affinities .
There are technologies that completely avoid the use of mice or other non-human mammals in the process of discovering antibodies for human therapy. Examples of such systems include various "display" methods (primarily phage display) as well as methods that exploit the elevated B-cell levels that occur during a human immune response.
It involves conjugating the phage library to the desired target. This procedure is termed panning. It utilizes the binding interactions so that only specific peptides presented by bacteriophage are bound to the target. For example, selecting antibody presented by bacteriophage with coated antigen in microtiter plates.
Internalizing RGD (iRGD) peptides are a class of 9-amino acid cyclic peptides containing an RGD sequence, which undergo internalization as discussed below. The prototypic iRGD peptide, shown in the image on the right (sequence: CRGDKGPDC; CAS 1392278-76-0), was originally identified in an in vivo screening of phage display libraries in tumor-bearing mice. [1]
John McCafferty is a British scientist, one of the founders of Cambridge Antibody Technology alongside Sir Gregory Winter and David Chiswell. He is well known as one of the inventors of scFv antibody fragment phage display, [1] a technology that revolutionised the monoclonal antibody drug discovery.
Bacterial display (or bacteria display or bacterial surface display) is a protein engineering technique used for in vitro protein evolution. Libraries of polypeptides displayed on the surface of bacteria can be screened using flow cytometry or iterative selection procedures (biopanning).
A single-domain antibody can be obtained by immunization of dromedaries, camels, llamas, alpacas or sharks with the desired antigen and subsequent isolation of the mRNA coding for the variable region (V NAR and V H H) of heavy-chain antibodies. Large phage displayed V NAR and V H H single domain libraries were established from nurse sharks [17 ...