Evaluation of Disulfide Bond Position to Enhance the Thermal Stability of a Highly Stable Single Domain Antibody

• Published in: PloS one Vol. 9; no. 12; p. e115405
• Main Authors: Zabetakis, Dan, Olson, Mark A., Anderson, George P., Legler, Patricia M., Goldman, Ellen R.
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 19.12.2014; Public Library of Science (PLoS)
• Subjects: Affinity; Analysis; Analytical chemistry; Animals; Antibodies; Antibody Affinity; Bioinformatics; Biology; Biology and Life Sciences; Calorimetry, Differential Scanning; Camelids, New World - immunology; Chemical bonds; Chromatography; Circular Dichroism; Crystal structure; Cysteine - genetics; Denaturation; Disulfide bonds; Disulfides - chemistry; Engineering; Enterotoxin B; Enterotoxins - metabolism; Immunoassay; Immunoglobulins; Immunology; Laboratories; Medicine and Health Sciences; Melting; Melting point; Melting points; Models, Molecular; Mutagenesis; Mutation; Nanobodies; Phase transitions; Physical Sciences; Protein denaturation; Protein expression; Protein folding; Protein Refolding; Protein Stability; Simulation; Single-Domain Antibodies - chemistry; Single-Domain Antibodies - genetics; Single-Domain Antibodies - metabolism; Solvents; Stability analysis; Staphylococcal enterotoxin A; Staphylococcal enterotoxin B; Temperature effects; Thermal stability; Transition Temperature

Single domain antibodies are the small recombinant variable domains derived from camelid heavy-chain-only antibodies. They are renowned for their stability, in large part due to their ability to refold following thermal or chemical denaturation. In addition to refolding after heat denaturation, A3,...