Experimental Elucidation of Templated Crystallization and Secondary Processing of Peptides

Author:

Verma Vivek1ORCID,Bade Isha1ORCID,Karde Vikram1,Heng Jerry Y. Y.12ORCID

Affiliation:

1. Department of Chemical Engineering, Imperial College London, London SW7 2AZ, UK

2. Institute for Molecular Science and Engineering, Imperial College London, London SW7 2AZ, UK

Abstract

The crystallization of peptides offers a sustainable and inexpensive alternative to the purification process. In this study, diglycine was crystallised in porous silica, showing the porous templates’ positive yet discriminating effect. The diglycine induction time was reduced by five-fold and three-fold upon crystallising in the presence of silica with pore sizes of 6 nm and 10 nm, respectively. The diglycine induction time had a direct relationship with the silica pore size. The stable form (α-form) of diglycine was crystallised in the presence of porous silica, with the diglycine crystals obtained associated with the silica particles. Further, we studied the mechanical properties of diglycine tablets for their tabletability, compactability, and compressibility. The mechanical properties of the diglycine tablets were similar to those of pure MCC, even with the presence of diglycine crystals in the tablets. The diffusion studies of the tablets using the dialysis membrane presented an extended release of diglycine through the dialysis membrane, confirming that the peptide crystal can be used for oral formulation. Hence, the crystallization of peptides preserved their mechanical and pharmacological properties. More data on different peptides can help us produce oral formulation peptides faster than usual.

Funder

Marie Sklodowska-Curie

Centre for Rapid Online Analysis of Reactions at Imperial College London

Publisher

MDPI AG

Subject

Pharmaceutical Science

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