![]() ![]() Responding to this challenge, we introduced an ensemble of peptide ligands that target the HCPs in Chinese hamster ovary (CHO) cell culture fluids and enable mAb purification via flow‐through affinity chromatography. Of special concern is the removal of “persistent” HCPs, including immunogenic and mAb‐degrading proteins, that co‐elute from the Protein A resin and can escape the polishing steps. The growth of advanced analytics in manufacturing monoclonal antibodies (mAb) has highlighted the challenges associated with the clearance of host cell proteins (HCPs). Our work resolves the physiological function of a ubiquitous protein modification and uncovers its crucial role in maintaining the structure and function of the bacterial membrane. Rapid membrane hyperpolarization and impaired membrane integrity were observed shortly after PDF inhibition and suggest that disruption of the plasma membrane is the most immediate and primary consequence of formyl group retention on nascent proteins. ![]() ![]() Loss of PDF activity rapidly induces cellular stress responses, especially those associated with protein misfolding and membrane defects, followed by a global downregulation of metabolic pathways. coli translatome and proteome to investigate the consequences of PDF inhibition. In this work, we used time-resolved analyses of the E. PDF is essential and a critical target of antibiotic development however, its role in bacterial physiology remains a long-standing question. Removal of the N-terminal formyl group on nascent proteins by peptide deformylase (PDF) is the most prevalent protein modification in bacteria. ![]()
0 Comments
Leave a Reply. |
AuthorWrite something about yourself. No need to be fancy, just an overview. ArchivesCategories |