期刊
MOLECULAR PHARMACEUTICS
卷 20, 期 11, 页码 5682-5689出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.molpharmaceut.3c00539
关键词
NMR spectroscopy; dynamic nuclear polarization; protein drug formulations; structure
Protein-based drug formulations pose challenges in terms of stability and morphology. This study used DNP NMR spectroscopy to determine the hierarchy of components within spray-dried particles containing protein, trehalose, leucine, and trileucine. The findings provide insights for rationalizing the performance of these formulations.
Protein-based drugs are becoming increasingly important, but there are challenges associated with their formulation (for example, formulating stable inhalable aerosols while maintaining the proper long-term stability of the protein). Determining the morphology of multicomponent, protein-based drug formulations is particularly challenging. Here, we use dynamic nuclear polarization (DNP) solid-state NMR spectroscopy to determine the hierarchy of components within spray-dried particles containing protein, trehalose, leucine, and trileucine. DNP NMR was applied to these formulations to assess the localization of the components within the particles. We found a consistent scheme, where trehalose and the protein are co-located within the same phase in the core of the particles and leucine and trileucine are distributed in separate phases at the surface of the particles. The description of the hierarchy of the organic components determined by DNP NMR enables the rationalization of the performance of the formulation.
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