Influence of Tableting on the Conformation and Thermal Stability of Trypsin as a Model Protein.
作者： Marten Klukkert , Marco van de Weert , Mathias Fanø , Thomas Rades , Claudia S. Leopold
DOI: 10.1002/JPS.24672
关键词: Protein structure 、 Protein secondary structure 、 Chemistry 、 Differential scanning calorimetry 、 Folding (chemistry) 、 Crystallography 、 Protein folding 、 Thermal stability 、 Tableting 、 Trypsin
摘要: The objective of this study was to investigate the influence compaction on conformation trypsin, its transition temperature (Tm ) unfolding, and folding reversibility after thermal denaturation. Plain trypsin compacted at 40-382 MPa. Pressure-induced changes in extent their were determined using solid- liquid-state IR spectroscopy together with principal component analysis an area overlap approach. Trypsin enzymatic activity by a photometric assay. Liquid-state differential scanning calorimetry performed determine Tm as well denaturation reconstituted samples. It found that samples showed reduced accompanied altered secondary structure. Conformational occur solid state partially reversible upon tablet reconstitution. Aqueous-state combined partial least squares shown be powerful tool follow irreversible structural evaluate sample bioactivity. Besides conformation, stability result applied pressure, indicated reversibility. In conclusion, reveals tableting can have negative impact biological quality protein APIs.
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