Custom designed oligopeptides are an increasingly accessible option in peptide-based technologies for pharmaceuticals. Following their synthesis, peptides are often subjected to HPLC purification and synthetic modification, which can require the use of non-aqueous media or salts requiring later removal. During the production of pharmaceutical peptides, spoilage can occur in the forms of aggregates, associates, and other means. Using ARGEN, we demonstrate the rapid formulation of four peptide solutions that are based on excipient effects correlated to increasing molecular weight. The first peptide was formulated in five days for optimal stability. The remaining three peptides were formulated in parallel over 10 days.
|Peptide||# of A.A.’s||Mass (Daltons)||Hydrophilicity||[Peptide] (mg/mL)||pH||[MeCN] (%)||[DMSO] (%)||[GnCl] (M)|
Table 1: Peptide characteristics and optimal conditions determined by rapid formulation with ARGEN. Exact amino acid sequences are not reported due to disclosure conditions with the supplier, but peptides are grouped by their reported hydrophilicity. Based on peptide primary structure, A-group peptides were predicted to be hydrophilic, and B-group peptides were predicted to be hydrophobic. Their excipient-dependent behavior was consistent with this designation. (%) is percent by volume. Peptide B-2 was not soluble enough to find an optimal peptide concentration for long-term storage. Peptide B-2’s poor solubility precluded it from a concentration study.