http://www-heparin.rpi.edu/main/files/papers/4e9b749fa0b173.58783057.pdf

N,N,N-Trimethyl chitosan nanoparticles for the delivery of monoclonal antibodies against hepatocellular carcinoma cells.

Selection strategies for anticancer antibody discovery: searching off the beaten path

The Cold Culture Wars: The Fight for Democratic Education in Post-War New York

/pdf/investigations-in-molecular-recognition-element-selection-33e5w4ajnw.pdf

Investigations in Molecular Recognition Element Selection and Single-Wall Carbon Nanotube Properties

Prostate cancer is the most-diagnosed non-skin cancer among males in the US, and the second leading cause of cancer-related death. Current methods of treatment and diagnosis are not specific for the disease. This work identified an antibody fragment that binds selectively to a molecule on the surface of androgen-dependent prostate cancer cells but not benign prostatic cells. Antibody fragment identification was achieved using a library screening and enrichment strategy. A library of 109 yeast-displayed human non-immune antibody fragments was enriched for those that bind to androgen-dependent prostate cancer cells, but not to benign prostatic cells or purified prostate-specific membrane antigen (PSMA). Seven rounds of panning and fluorescence-activated cell sorting (FACS) screening yielded one antibody fragment identified from the enriched library. This molecule, termed HiR7.8, has a low-nanomolar equilibrium dissociation constant (Kd) and high specificity for androgen-dependent prostate cancer cells. Antibody fragment screening from a yeast-displayed library has yielded one molecule with high affinity and specificity. With further pre-clinical development, it is hoped that the antibody fragment identified using this screening strategy will be useful in the specific detection of prostate cancer and in targeted delivery of therapeutic agents for increased efficacy and reduced side effects.

/pdf/identification-of-an-antibody-fragment-specific-for-androgen-2caetu0u78.pdf

Identification of an antibody fragment specific for androgen-dependent prostate cancer cells

Analysing protein-protein interactions is critical in proteomics and drug discovery. The usage of 2-Hybrid (2lambda) systems is limited to an in vivo environment. We describe a bacteriophage 2-Hybrid system for studying protein interactions in vitro. Bait and prey are displayed as fusions to the surface of phage lambda that are marked with different selectable drug-resistant markers. An interaction of phages in vitro through displayed proteins allows bacterial infection by two phages resulting in double drug-resistant bacterial colonies at very low multiplicity of infections. We demonstrate interaction of the protein sorting signal Ubiquitin with the Vps9-CUE, a Ubiquitin binding domain, and by the interaction of (Gly-Glu)(4) and (Gly-Arg)(4) peptides. Interruptions of the phage interactions by non-fused (free) bait or prey molecules show how robust and unique our approach is. We also demonstrate the use of Ubiquitin and CUE display phages to find binding partners in a lambda-display library. The unique usefulness to 2lambda is also described.

https://onlinelibrary.wiley.com/doi/pdf/10.1111/j.1365-2958.2007.06077.x

A phage display system designed to detect and study protein-protein interactions.

Human scFv antibody fragments specific for hepatocellular carcinoma selected from a phage display library

Wen-Han Li

Papers

Human scFv antibody fragments specific for hepatocellular carcinoma selected from a phage display library.