The process using a synthetic library that generates multiple diverse human single domain antibodies.

Background: Single domain antibodies (sdAbs) possess unique characteristics that make them highly effective for developing complex therapeutics.

Methods: Our process uses a fully synthetic phage display library to generate single domain antibodies that can bind to disease relevant antigen conformations. A human IGHV3 family scaffold makes up the phage display libraries, and these VHO libraries are applied to diverse phage biopannings against target antigens.

Impact of tetracycline-clay interactions on bacterial growth.

Antibiotics are extremely effective against bacterial infections due to their selective toxicity for bacteria rather than the host. Extensive use and misuse of antibiotics resulted in significant increases in antibiotic levels in aquatic and soil environments. Bacteria exposed to antibiotics with low concentrations may develop antibiotic resistance.

Over-expression, solubilization, and purification of G protein-coupled receptors for structural biology.

With the advent of the recent determination of high-resolution crystal structures of bovine rhodopsin and human beta2 adrenergic receptor (beta2AR), there are still many structure-function relationships to be learned from other G protein-coupled receptors (GPCRs). Many of the pharmaceutically interesting GPCRs cannot be modeled because of their amino acid sequence divergence from bovine rhodopsin and beta2AR. Structure determination of GPCRs can provide new avenues for engineering drugs with greater potency and higher specificity.