Solubility Optimization

Legacy BioDesign has been successful in identifying solution conditions that will promote increased solubility for both peptides and proteins. Using self-interaction chromatography (SIC), one can use conventional HPLC equipment to measure protein-protein interactions (known as the second osmotic virial coefficient or B value). These values are known to correlate with solubility as well as decreased propensity to aggregate. We have used SIC for our clients, covering a wide range of polypeptides from small peptides to monoclonal antibodies. Furthermore, it should be noted that SIC is the only method available to measure B values for peptides. In collaboration with Professor Charles Henry at Colorado State University, we have published a number of studies demonstrating the utility of the SIC approach.

 

Publications

“Self-Interaction Chromatography for Screening”, Charles S. Henry, Robert W. Payne, Joseph J. Valente, William W. Wilson, and Mark Cornell Manning, Genetic Eng. News 2005, 25: 62-63.

 

“Colloidal Behavior of Proteins: Effects of the Second Virial Coefficient on Solubility, Crystallization, and Aggregation of Proteins in Aqueous Solution”, Joseph J. Valente, Robert W. Payne, Mark Cornell Manning, W. William Wilson and Charles S. Henry, Current Pharm. Biotechnol. 2005, 6: 427-436.

 

“Towards the Systematic Use of Virial Coefficient Studies for Evaluating Cosolvent-Induced Stabilization and Solubilization of Proteins”, Joseph J. Valente, Kusum Verma, Mark Cornell Manning, W. William Wilson, and Charles S. Henry, Biophys. J. 2005, 89: 4211-4218.

 

“Second Virial Coefficient Determination of a Therapeutic Peptide by Self-Interaction Chromatography”, Robert W. Payne, Rajiv Nayar, Ralph Tarantino, Sam Del Terzo, John Moschera, Jie Di, David Heilmann, Brian Bray, Mark Cornell Manning, and Charles S. Henry, Biopolymers (Peptide Science) 2006, 84: 527-533.