A comparison of strategies to stabilize immunoglobulin Fv-fragments
Citations Over TimeTop 1% of 1990 papers
Abstract
Fv-Fragments of antibodies may dissociate at low protein concentrations and are too unstable for many applications at physiological temperatures. To stabilize Fv-fragments against dissociation, we have tested and compared three different strategies on the Fv-fragment of the well-characterized phosphocholine binding antibody McPC603 expressed and secreted in Escherichia coli: chemical cross-linking of the variable domains, introduction of an intermolecular disulfide bond, and construction of a peptide linker to produce a "single-chain" Fv-fragment. All the linked fragments show hapten affinities nearly identical with that of the whole antibody independent of protein concentration and are significantly (up to 60-fold) stabilized against irreversible thermal denaturation. All genetically engineered linked Fv-fragments can be obtained in native conformation in E. coli. The reported strategies for generating Fv-fragments with improved physicochemical properties may extend their usefulness in biotechnology as well as in therapeutic and diagnostic applications.
Related Papers
- → Citations Gone #Social: Examining the Effect of Altmetrics on Citations and Readership in Communication Research(2019)27 cited
- → Honoring Native American Code Talkers(2011)5 cited
- → From Attention to Citation, What and How Does Altmetrics Work?(2014)20 cited
- → Literature(1998)1 cited
- Susquehanna Chorale Spring Concert "Roots and Wings"(2017)