Rachel Baribault Kent

TL;DR: The construction of human Fab libraries having a unique combination of immunoglobulin sequences captured from human donors and synthetic diversity in key antigen contact sites in heavy-chain complementarity-determining regions 1 and 2 are reported.

TL;DR: A series of new technologies have recently been developed that allow peptides to be viable drug candidates in areas usually restricted to protein therapeutics, such as monoclonal antibodies, and have helped to improve peptide stability and further their therapeutic potential.

TL;DR: The discovery of ACE2 peptide inhibitors through selection of constrained peptide libraries displayed on phage demonstrates that library selection by phage display technology can be a rapid and efficient way to discover potent and specific protease inhibitors.

TL;DR: Several phage isolates that bind specifically to human serum albumin were isolated from disulfide‐constrained cyclic peptide phage‐display libraries and one of the highest affinity peptides, DX‐236, also bound well to several mammalian serum albumins (SA).

TL;DR: In this article, the CD44-binding proteins, including CD44 binding antibodies, antibody fragments, and pharmaceutical compositions thereof, as well as nucleic acids, recombinant expression vectors and host cells for making such proteins are described.