Eunji Park
Kyung Hee University · 医学
研究室紹介
Professor Eunji Park's research lab specializes in pharmaceutical and biotechnological innovation, with a primary focus on peptide and protein drug delivery systems, particularly the development of orally available peptide therapeutics. The lab investigates advanced drug modification technologies such as PEGylation to enhance the stability, solubility, and bioavailability of therapeutic peptides and proteins. Additionally, the lab explores analytical challenges in characterizing PEGylated biomolecules using techniques like RP-HPLC and microchip CGE, aiming to improve separation and purification processes. Environmental sustainability in healthcare is also a growing research interest, particularly the ecological impact of anesthetic agents in operating rooms.
Research Overview
Research Output Trend
Figures are computed from collected data and may differ slightly.
Selected Papers
15<b>Introduction</b>: PEGylation is a well-established technology for improving the therapeutic value of drugs by attaching polyethylene glycol (PEG). The first PEGylated enzyme products appeared on the market in the early 1990s; currently, more than 18 PEGylated products have been approved by Food and Drug Administration, which encompass various classes of drug molecules, such as enzymes, interferons, granulocyte colony-stimulating factors, hormones, antibody fragments, coagulation factors, olig
Recently, two oral-administered peptide pharmaceuticals, semaglutide and octreotide, have been developed and are considered as a breakthrough in peptide and protein drug delivery system development. In 2019, the Food and Drug Administration (FDA) approved an oral dosage form of semaglutide developed by Novo Nordisk (Rybelsus®) for the treatment of type 2 diabetes. Subsequently, the octreotide capsule (Mycapssa®), developed through Chiasma’s Transient Permeation Enhancer (TPE) technology, also re
Recently, research on exendins and their analogs has grown significantly, leading to the development of long-acting analogs and multifunctional peptides. While long-acting injectable agents are still the major products in the pharmaceutical industry, a significant growth is expected in the development of orally available exendins.
The separation mechanism of PEGylated peptides in reversed-phase high-performance liquid chromatography (RP-HPLC) is complex, because the PEGylated molecules exhibit physicochemical properties that are different from those of the parent molecules and have heterogeneous structure. Since most separation studies have focused on the hydrophobicity of the peptide relative to poly(ethylene glycol) (PEG), the role of PEG in the separation of PEGylated peptides on RP-HPLC is not clear. To elucidate the
The objective of this study was to characterize the differences in electrophoretic behavior between linear and branched PEG-conjugated proteins. Human growth hormone and alpha-lactalbumin modified by linear or branched PEGs with molecular weight of 10 kDa were analyzed by SEC, MALDI-TOF MS, SDS-PAGE, and microchip CGE (MCGE). Chromatographic and mass spectrometric differences between the linear and branched PEG-proteins on SEC and MALDI-TOF MS were small, but their electrophoretic behaviors on S
Environmental concerns, especially global warming, have prompted efforts to reduce greenhouse gas emissions. Healthcare systems, including anesthesia practices, contribute to these emissions. Inhalation anesthetics have a significant environmental impact, with desflurane being the most concerning because of its high global warming potential. This study aimed to educate anesthesiologists on the environmental impact of inhalation anesthetics and assess changes in awareness and practice patterns, s
Abstract The purpose of this study was to investigate the effect of pH on the complexation of quercetin and polyamidoamaine (PAMAM) dendrimers, which can exert antioxidant activity in aqueous solution. The therapeutic use of quercetin has been limited due to its low water solubility and bioavailability. In this study, quercetin was complexed with generation 4 PAMAM (G4) in different buffers at pH 4–9, with pH 6 showing the best results in terms of solubility and stability. The solubility of quer