Stability Enhancing N-Terminal PEGylation of Oxytocin Exploiting Different Polymer Architectures and Conjugation Approaches

n-terminal pegylation of recombinant human erythropoetin and evaluation of its biological activity and physicochemical stability

N-terminal PEGylation of human serum albumin and investigation of its pharmacokinetics and pulmonary microvascular retention.

Human serum albumin (HSA) is used as an important plasma volume expander in clinical practice. In the present study, HSA was N-terminally PEGylated and a PEGylated HAS (PEG-HSA) carrying one chain of PEG (20 kDa) per HSA molecule was obtained. The purity, secondary structure and hydrodynamic radius of the modified protein were characterized using sodium dodecyl sulfate polyacrylamide gel electr...

Pegylation of Peptides the Case for Peg Conjugation

Site – specific PEGylation of rHuEPO and evaluation of its biological activity and stability

Despite the critical role of erythropoietin (EPO) as therapeutic agent in treatment of anemia, its consumption is limited due to several disadvantages including the product short half-life, immunogenicity and susceptibility to proteolytic degradation. To overcome these drawbacks efficient methods such as site-specific PEGylation have been developed among witch N-terminal PEGylation has found mo...

Intrinsic bioconjugation for site-specific protein PEGylation at N-terminal serine.

Recently developed chemical ligation protocols were elaborated for rapid N-terminal protein PEGylation. We introduce a PEG-salicylaldehyde ester and demonstrate its site-specific ligation to the N-terminus of the RNase S protein and to the therapeutic polypeptide PTH (1-34).