Although low molecular weight means less complexity, peptide-based therapeutics are by no means a product that's easy to develop.
Overcoming an inherently low stability, which contributes to rapid degradation and clearance in-vivo, and being in control of self-aggregation demands for characterization techniques that reliably monitor structural integrity. CD spectroscopy is well-suited for this purpose, and Chirascan systems provide the required sensitivity.
This examplary study aimed at finding a suitable formulation for the GLP-1-like peptide G48.
By monitoring peptide structure with a Chirascan system and evaluation at a range of conditions, including different concentrations, pH values, and excipients, it was found that undesired peptide fibrillation was successfully inhibited in presence of polysorbate 80.
Moreover, CD data reveals that peptide aggregation depends on net charge, as different magnitudes of structural changes are observed at neutral pH as compared to acidic or basic pH.
See the original paper for this study here.