원문정보
초록
영어
Covalent conjugation of poly(ethylene glycol) (PEG) to therapeutic proteins increases their in vivo stability by protecting the protein from degradation, masking its immunogenic sites and reducing clearance1). Frequently, PEGylation results in non-site specificity and multiple attachments, which might mask or interfere with the receptor binding sites, causing a dramatic
decrease in in vitro bioactivity. To solve this problem, site-specific PEGylation has been employed2). Epidermal growth factor (EGF) has been used as a medical treatment, since it controls and accelerates the epidermal cell's proliferation3). In this study, we demonstrated the PEGylation of the thiolated EGF using 2․iminothiolane․HCl, which can improve the binding
interaction between a PEG molecule and a EGF protein and yield of the PEGylation. The site of PEGylation was identified through tryptic peptide mapping and Matrix Assisted Laser Desorption-Time of Flight (MALDI-TOF) techniques, which shows mass analysis and identified through Reversed Phase-HPLC, which can confirm the existence of tri-, di-, mono-EGF PEGylates and their purity levels.