Sampathkumar Krishnan

TL;DR: The purpose of the current review is to provide a fundamental understanding of the mechanisms by which proteins aggregate and by which varying solution conditions, such as temperature, pH, salt type, salt concentration, cosolutes, preservatives, and surfactants, affect this process.

TL;DR: Non‐native aggregation of recombinant human granulocyte stimulating factor (rhGCSF) in solution conditions where native rhG CSF is both conformationally stable compared to its unfolded state and at concentrations well below its solubility limit is studied.

TL;DR: A formulation strategy involving optimization of colloidal stability of the antibody as well as incorporation of surfactants such as polysorbate 20 is proposed to reduce silicone oil-induced aggregation of therapeutic protein products.

TL;DR: This work has found that the critical rate-limiting step in nucleation of alpha-synuclein fibrils under physiological conditions is the oxidative formation and accumulation of a dimeric, dityrosine cross-linked prenucleus, which supports a mechanism of Parkinson's disease pathogenesis in which the separately studied pathogenic factors of oxidative stress and alpha- synuclein aggregation converge at the critical step ofalpha-syn DNA dimer formation.

TL;DR: Investigation of the aggregation of recombinant human granulocyte colony stimulating factor finds that native monomeric rhGCSF reversibly forms a dimer under physiological conditions and that this dimeric species does not participate in the irreversible aggregation process, and proposes that sucrose, a thermodynamic stabilizer, inhibits the aggregation.