Probing the mechanism of insulin aggregation during agitation

摘要: Abstract Agitation of insulin during its storage and transport has been reported to denature the protein, resulting in inactivation. The physical changes accompanying denaturation process which result aggregation are poorly understood. In this work, we study aggregates formed following agitation under defined conditions by different chemical techniques. We show that both non-disulphide-mediated covalent bonds as well non-covalent interactions involved formation aggregates. two-step kinetics could be clearly seen, with discrete ‘early’ ‘late’ stages fibrillation. Understanding nature agitation-induced will help devising a strategy protect therapeutic protein against instability transport.