(438d) Crystallisation of Short Peptides | AIChE

(438d) Crystallisation of Short Peptides

Authors 

Chen, W. - Presenter, Imperial College London
Heng, J. Y. Y., Imperial College London
Chan, X. S., Imperial College London
Guo, M., Imperial College London
Yang, H., Imperial College London
Bio-active peptides can be used as highly effective pharmaceutical compounds to treat a wide range of diseases. The purification of peptide currently relies on chromatography which contributes significantly to the high cost of downstream processing. Although crystallisation is a more economical and scalable option for the purification of peptide, there is a knowledge gap in peptide crystallisation which the current study aims to fill by investigating the crystallisation of short peptides that have less than 10 amino acids in a sequence. Since the measurement of solubility is the first step in the development of a crystallisation strategy, the solubility of short peptides such as aspartame and polyglycines between 5 and 40 degrees Celcius is determined before performing the crystallisations. The experimental data of this study not only confirms the feasibility of peptide crystallisation over a range of conditions, but are also useful for constructing thermodynamic models for predicting the solubility of short peptides in the future studies. The knowledge of this work can aid the downstream processing of bio-active peptides in general.

Acknowledgement

We acknowledge the EPSRC (EP/N015916/1) for funding.

Reference

  1. Kastin, A. Handbook of Biologically Active Peptides. Academic press (2013).
  2. IUPAC‐IUB Joint Commission on Biochemical Nomenclature (JCBN) Nomenclature and Symbolism for Amino Acids and Peptides Recommendations 1983. Int. J. Pept. Protein Res. 24, 9–37 (1984).