Young‐Pil Kim
Hanyang University · 生化学・遺伝学・分子生物学
研究室紹介
Professor Young-Pil Kim's research lab specializes in the development of innovative nanomaterial-based platforms for biomedical diagnostics and therapeutics. The lab focuses on designing smart bio/nanomaterials for targeted cancer therapy, particularly through photodynamic therapy (PDT) and bioluminescence-mediated strategies. Key research directions include the engineering of quantum dots, gold nanoparticles, and protein conjugates for sensitive detection of proteases, kinase activity, and glycosylation, as well as for real-time, label-free imaging and theranostic applications. The lab integrates principles of bioconjugation, energy transfer, and molecular imaging to create next-generation tools for precision medicine.
Research Overview
Research Output Trend
Figures are computed from collected data and may differ slightly.
Selected Papers
15Photodynamic therapy (PDT) has been considered a noninvasive and cost-effective modality for tumor treatment. However, the complexity of tumor microenvironments poses challenges to the implementation of traditional PDT. Here, we review recent advances in PDT to resolve the current problems. Major breakthroughs in PDTs are enabling significant progress in molecular medicine and are interconnected with innovative strategies based on smart bio/nanomaterials or therapeutic insights. We focus on newl
Rapid and sensitive assay of proteases and their inhibition in a high-throughput manner is of great significance in the diagnostic and pharmaceutical fields. We developed a multiplexed assay system of proteases and their inhibition by measuring the energy transfer between quantum dots (QDs) and gold nanoparticles (AuNPs) on a glass slide. In this system, while the photoluminescence (PL) of donor QDs immobilized on a surface was quenched due to the presence of AuNPs (energy acceptor) in close pro
This communication reports the use of click chemistry to site-specifically conjugate bioluminescent Renilla luciferase proteins to gold nanoparticles (Au NPs) for sensing protease activity. The bioluminescent emission from luciferase was efficiently quenched by Au NPs, but significantly recovered after the proteolytic cleavage.
Spot the mass of peptides: A label-free protein kinase assay that uses secondary-ion mass spectrometric imaging has been demonstrated with peptide-conjugated gold nanoparticles (AuNPs). With detection of the mass change of peptide substrates in a kinase reaction, AuNP-enhanced peptide signals enabled the assaying of both the protein kinase and its inhibition by chemical imaging of peptide substrates on a surface (see picture).
Photoluminescence quenching of dextran-conjugated quantum dots (dex-QDs) by gold nanoparticles conjugated with concanavalin A (conA-AuNPs) can be prevented by adding a glycoprotein, which inhibits the association of dex-QDs with conA-AuNPs (see scheme). This phenomenon can be used as an analytical tool for the detection of protein glycosylation. PL=photoluminescence.
as a substrate for luciferase without external light irradiation, Luc-RGP fused with a small lead peptide-induced breast cancer cell death through the generation of BL-sensitive ROS in the plasma membrane. Even with extremely low light energy, BLiP-PDT exhibited targeted effects in primary breast cancer cells from patients and in in vivo tumor xenograft mouse models. These findings suggest that BLiP-PDT is immediately useful as a promising theranostic approach against various cancers.
We demonstrate the effects of protein orientation and trehalose on a quantitative analysis of surface-immobilized proteins by using time-of-flight secondary ion mass spectrometry (TOF-SIMS). As our model protein, streptavidin (SA) was quantitatively immobilized on a solid surface at different configurations by random or oriented immobilization and subsequently treated with trehalose. The resulting surface was analyzed by using TOF-SIMS and surface plasmon resonance (SPR) spectroscopy, where the
We demonstrate the use of gold nanoparticles (AuNPs) to enhance the secondary ion emission of peptides in time-of-flight secondary ion mass spectrometry (TOF-SIMS). The signal intensity of peptides adsorbed onto AuNPs was significantly increased when compared to that of self-assembled monolayers (SAMs). This gold nanoparticle-enhanced SIMS, termed NE-SIMS, enabled the sensitive detection of subtle modifications of peptides, such as phosphorylation. From a quantitative analysis of the amounts of
Bio-conjugated nanoparticles have emerged as novel molecular probes in nano-biotechnology and nanomedicine and chemical analyses of their surfaces have become challenges. The time-of-flight (TOF) secondary ion mass spectrometry (SIMS) has been one of the most powerful surface characterization techniques for both nanoparticles and biomolecules. When combined with various nanoparticle-based signal enhancing strategies, TOF-SIMS can probe the functionalization of nanoparticles as well as their loca
Detection and characterization of cells using aptamers and aptamer-conjugated nanoprobes has evolved a great deal over the past few decades. This evolution has been driven by the easy selection of aptamers via in vitro cell-SELEX, permitting sensitive discrimination between target and normal cells, which includes pathogenic prokaryotic and cancerous eukaryotic cells. Additionally, when the aptamer-based strategies are used in conjunction with nanomaterials, there is the potential for cell target
A label-free, activity-based assay of matrix metalloproteinase (MMP) and its inhibition was demonstrated on peptide-conjugated gold nanoparticles (AuNPs) with nonbiofouling poly(oligo(ethylene glycol) methacrylate) (pOEGMA) films using time-of-flight secondary ion mass spectrometry (TOF-SIMS). Following surface-initiated atom-transfer radical polymerization of OEGMA on a Si/SiO2 substrate, the MMP activity was determined by analyzing the cleaved peptide fragments using TOF-SIMS on the peptide-co