ポスター：バイオ医薬品におけるスクランブルされたジスルフィド結合の自動かつ堅牢な同定

ASMS 2024, Anaheim, CA, USA
June 2, 2024

Disulfide bonds are covalent bonds that form between two cysteine amino acids in a protein chain and are unique among post-translational modifications (PTMs), as they add covalent cross-links to the polypeptide chain. In some biopharmaceuticals, the arrangement of disulfide bonds can be changed, leading to dislocated linkages, a process often referred to as being “scrambled”. This scrambling can occur at any stage of the manufacturing process from expression to final formulation or be an artefact of sample preparation. Monitoring the proportion of scrambled disulfide bonds is critical for ensuring the structural stability and functional integrity — and hence the safety and efficacy — of therapeutic proteins.