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Biotech / Medical : HuMAB companies -- Ignore unavailable to you. Want to Upgrade?

To: tnsaf who wrote (1010)	8/26/2014 7:57:03 AM
From: nigel bates	Respond to of 1022

Generation, characterization and structural data of chymase binding proteins based on the human Fyn kinase SH3 domain ncbi.nlm.nih.gov "...Antibodies and antibody fragments are routinely employed for analytical, purification, diagnostic and therapeutic purposes because of their high affinity and specificity to virtually any desired target antigen, but they still have a number of serious drawbacks, such as the need for complex mammalian cell production systems, a dependency on disulfide bonds for stability, and the tendency of some antibody fragments to aggregate, which limits solubility. As a consequence, novel classes of versatile binding proteins using small globular proteins as scaffolds have been generated. Typically, surface components (e.g., extracellular loops) of a protein framework with suitable biophysical properties are combinatorially mutated to produce a diverse protein library to be screened for specific binding to the target of interest. More than 50 different protein scaffolds have been proposed over the past 10 to 15 y, the most advanced of which are affibodies (based on the Z- domain of staphylococcal protein A), Kunitz type domains, Adnectins (based on the 10th domain of human fibronectin), Anticalins (derived from lipocalins), DARPins (derived from ankyrin repeat proteins), avimers (based on multimerized LDLR-A) and Fynomers, which are derived from the human Fyn SH3 domain. The Fyn SH3 domain is a particularly attractive scaffold for the generation of binding proteins because the resulting “Fynomer” (1) can be expressed in bacteria in soluble form in high amounts, (2) is monomeric and does not aggregate when stored in solution, (3) is very stable (Tm ~70°C), (4) lacks cysteine residues, and (5) is of human origin featuring an amino acid sequence completely conserved from mouse to man and, hence, is considered to be non-immunogenic..."