By Prof. Jerry Heng, Ph.D.
Professor, Department of Chemical Engineering at Imperial College

The purification of high molecular weight new modalities such as peptides, for their use in biopharmaceutical drug therapeutics, can still account for a significant proportion of the drug development cost. Crystallisation can be an attractive isolation step for pharmaceutical products due to its unique ability to purify and control other properties such as particle size distribution, morphology, and polymorphism. This talk will focus on my group’s recent efforts to control nucleation and crystallisation of peptides. The effects of chain length on solubility and crystallisation kinetics are determined for glycine homopeptides as a model system. The solubility study is extended for the simple peptides in single and binary solvent mixtures (water-ethanol, water-DMSO), to include the effect of sequence (eg gly-ala, ala-gly) and protection groups on solubility of peptides, and finally discussing their crystallisation behaviour in the absence and presence of templates. The use of soft templates (eg amino acids) for a model peptide/protein (insulin) will be presented. This talk will provide some insights into the challenges and opportunities in crystallisation as a purification unit process for peptides