Proteins and Peptides: Pharmacokinetic, Pharmacodynamic, and by Randall J. Mrsny, Ann Daugherty
By Randall J. Mrsny, Ann Daugherty
Addressing the elevated use of protein and peptide applicants as remedies for formerly untreatable illnesses, this accomplished and innovative resource presents the reader with a roadmap to an elevated realizing of matters serious for effectively constructing a protein or peptide healing candidate. Proteins and Peptides is a useful resource for drug discovery and improvement scientists within the biopharmaceutical who usually navigate the maze of protein and peptide pharmacokinetics, pharmacodynamics, and metabolism. Key gains contain:
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Additional info for Proteins and Peptides: Pharmacokinetic, Pharmacodynamic, and Metabolic Outcomes (Drugs and the Pharmaceutical Sciences)
Several investigators have similarly demonstrated that modification of the net charge of an Ab also correlates with an altered PK without affecting the in vitro antigen binding. For instance, Lee and Pardridge have related the immunoreactivities of charge-modified anti–epidermal growth factor receptor (EGFR) Abs to their PK profiles (80). The 528 murine mAb recognizing the human EGFR was sequentially cationized with hexamethylenediamine and conjugated with diethylenetriaminepentaacetic acid (DTPA) as a potential radioimmunoconjugate for imaging EGFR-expressing cancer (80).
Andrew Boswell, Rong Deng, Kedan Lin, Wendy S. Putnam, Cherry Lei, Frank-Peter Theil, Amita Joshi, Paul J. Fielder, and Leslie A. A. INTRODUCTION In contrast to small molecular weight drugs (SMD), the development of in vitro– in vivo correlations (IVIVCs) for monoclonal antibody (mAb) therapeutics is still in its infancy. High-throughput in vitro assays with established IVIVC that currently exist for SMD have not been so strongly pursued for antibody (Ab) therapeutics, reflecting to a certain degree the substantially lower attrition rate and the associated lower numbers of potential clinical mAb candidates.
Dennis et al. demonstrated that the clearance of an Fab fragment can be dramatically decreased through association with albumin (71). They developed one high-affinity AB peptide and fused it to an anti-tissue factor Fab D3H44. 8 hours for Fab D3H44 in rabbits (71). Building on Dennis’s work, Nguyen et al. found that the PK of an anti–human epidermal growth factor receptor 2 (HER2) AB-Fab 4D5 could be modulated as a function of affinity for albumin (72). 5 mM) and clearance (ranging over *50-fold in rats and *20-fold in rabbits) for AB-Fab variants (72).