Dissociation mechanics and stability of type A botulinum neurotoxin complex by means of biophysical evaluation
نویسندگان
چکیده
Biophysical characterisation of type A botulinum neurotoxin (BoNT/A) could be challenging since it exists in association with associated proteins (NAPs) as large protein complexes. The objective this study was to elucidate the dissociation mechanics BoNT/A complex along its thermodynamic stability through a combination analytical tools. Size exclusion chromatography (SEC) mainly used behavior at various pH. In addition, multi-angled light scattering (MALS), enzyme linked immunosorbent assay (ELISA), and dynamic (DLS) were utilized validate chromatographic results. from found strongly dependent on pH higher towards alkaline which further accelerated time temperature. dissociated 7.4 showed lower thermal compared state even presence polysorbate, revealed by SEC chromatogram aggregation onset Moreover, partial reversibility after titration 6.0, suggested vulnerability formation irreversible aggregates dissociates, signifying profile dissociation. Overall, more stable when NAPs 6.0 7.4. conventional relatively quantify amount different formulations.
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ژورنال
عنوان ژورنال: Journal of Pharmaceutical Investigation
سال: 2022
ISSN: ['2093-6214', '2093-5552']
DOI: https://doi.org/10.1007/s40005-022-00570-2