@article{eec5cff9-3b2a-4e31-9bff-e619297d0725,
  abstract     = {{<p>The stability of therapeutic proteins is crucial for maintaining their efficacy and safety. Misfolded or aggregated proteins can accelerate aggregation by a seeding effect, altering protein stability and interactions. Heat-induced aggregates can pose a risk because they can have perturbed structures that expose aggregate-prone regions. This study explored seeding by heat-induced protein aggregates on the stability and aggregation of two therapeutic proteins, human growth hormone (hGH) and a monoclonal Antibody (Antibody A), during storage of two weeks at three relevant temperatures of 4 °C, room temperature (RT, 21-23 °C), and 40 °C. Grwoth of aggregates were seen in the sub-micron-sized aggregates by Dynamic Light Scattering at 4 °C or RT. Furthermore, heated Antibody A showed signs of reversibility of higher-order structure after storage. Samples stored at 4 °C and RT showed similar stability and aggregation behaviour. While two weeks of storage at 40 °C accelerated the structural degradation of both proteins, it did not accelerate aggregation or particle formation for either hGH or Antibody A.</p>}},
  author       = {{Västberg, Amanda and Markova, Natalia and Nilsson, Lars and King, Patrick and Schaefer, Jan and Sivakumar, Balasubramanian and Sjögren, Helen and Wahlgren, Marie and Elofsson, Ulla}},
  issn         = {{1773-2247}},
  keywords     = {{Heat-induced aggregation; Human growth hormone; Monoclonal antibody; Seeding}},
  language     = {{eng}},
  publisher    = {{Editions de Sante}},
  series       = {{Journal of Drug Delivery Science and Technology}},
  title        = {{Effect of aggregate seeding on protein stability in solution}},
  url          = {{http://dx.doi.org/10.1016/j.jddst.2026.108193}},
  doi          = {{10.1016/j.jddst.2026.108193}},
  volume       = {{120}},
  year         = {{2026}},
}