Yongho Kim
Sungkyunkwan University · Materials Science
About the Lab
Professor Yongho Kim's research lab specializes in the intersection of bioelectronics, protein engineering, and nanomaterials for next-generation healthcare and biocatalysis. The lab focuses on designing intelligent bioelectronic systems for real-time, patient-friendly health monitoring and treatment, leveraging wearable and implantable technologies. A key research direction involves the rational design of peptides and proteins to direct the self-assembly of nanomaterials—such as C60 fullerenes and graphene—into highly ordered, functional superstructures with tailored electronic and structural properties. The lab also applies computational modeling and machine learning to optimize biomolecular systems for applications in energy, pharmaceuticals, and structural biology.
Research Overview
Research Output Trend
Figures are computed from collected data and may differ slightly.
Selected Papers
15Abstract Since the beginning of human history, the demand for effective healthcare systems for diagnosis and treatment of health problems has grown steadily. However, traditional centralized healthcare requires hospital visits, making in‐time and long‐term healthcare challenging. Bioelectronics has shown potential in patient‐friendly healthcare owing to the rapid advances in diverse fields of biology and electronics. In particular, wearable and implantable bioelectronics have emerged as an alter
Learning to engineer self-assembly would enable the precise organization of molecules by design to create matter with tailored properties. Here we demonstrate that proteins can direct the self-assembly of buckminsterfullerene (C60) into ordered superstructures. A previously engineered tetrameric helical bundle binds C60 in solution, rendering it water soluble. Two tetramers associate with one C60, promoting further organization revealed in a 1.67-Å crystal structure. Fullerene groups occupy peri
This article reviews the integration of multidisciplinary approaches, including protein engineering, computational biology, and nanoarchitectonics, to advance pharmaceutical enzyme biocatalysis.
We present a strategy for designed self-assembly of peptides into two-dimensional monolayer crystals on the surface of graphene and graphite. As predicted by computation, designed peptides assemble on the surface of graphene to form very long, parallel, in-register β-sheets, which we call β-tapes. Peptides extend perpendicularly to the long axis of each β-tape, defining its width, with hydrogen bonds running along the axis. Tapes align on the surface to create highly regular microdomains contain
Several phenomena occurring throughout the life of living things start and end with proteins. Various proteins form one complex structure to control detailed reactions. In contrast, one protein forms various structures and implements other biological phenomena depending on the situation. The basic principle that forms these hierarchical structures is protein self-assembly. A single building block is sufficient to create homogeneous structures with complex shapes, such as rings, filaments, or con
Theranostic platforms have emerged as advanced systems integrating diagnostic and therapeutic agents to enable personalized medicine tailored to the specific characteristics of each patient's disease. However, conventional theranostic strategies face challenges in achieving high specificity and sensitivity for diagnosis and therapy. This necessitates the development of novel platforms to improve diagnostic accuracy and therapeutic efficacy. Peptide-nanoparticle conjugates (PNCs) have recently ga
Polydimethylsiloxane (PDMS) was coated on multi-walled carbon nanotubes (MWCNTs) using a chemical vapour deposition method, and the PDMS-coated MWCNTs were well dispersed in various solvents without additional dispersants. Spin casting of the MWCNT-containing solution on a substrate pre-treated with PDMS-SiO2 nanoparticles resulted in the formation of a uniform thin film. The resulting thin film containing MWCNTs showed high optical transparency, conductivity and superhydrophobicity. We demonstr
Peptide assemblies have received significant attention because of their important role in biology and applications in bionanotechnology. Despite recent efforts to elucidate the principles of peptide self-assembly for developing novel functional devices, peptide self-assembly on two-dimensional nanomaterials has remained challenging. Here, we report nature-inspired two-dimensional peptide self-assembly on pristine graphene via optimization of peptide–peptide and peptide–graphene interactions. Two
A transient cytosolic delivery system for accurate Cas9 ribonucleoprotein is a key factor for target specificity of the CRIPSR/Cas9 toolkit. Owing to the large size of the Cas9 protein and a long negative strand RNA, the development of the delivery system is still a major challenge. Here, a size-controlled lipopeptide-based nanosome system is reported, derived from the blood-brain barrier-permeable dNP2 peptide which is capable of delivering a hyperaccurate Cas9 ribonucleoprotein complex (HypaRN
Abstract Transition metal dichalcogenides (TMDC) exhibit highly superior electrical properties and are typically obtained through mechanical exfoliation. This method has significant limitations, however, such as patterning issues and non‐uniformity, which hinder their application in integrated circuits as transistors and array pixel displays. To overcome these challenges, various large‐scale deposition methods have been developed. In this review, we introduce five major methods for TMDC depositi
현재 법원에서의 디지털저장매체의 압수방법과 관련하여 형소법 제106조제3항에서 제시하는 원칙적 선별압수,예외적인 매체압수 방식은 실제의 수사현실을 무시한 것이며, 이것을 준수하여 집행하기에는 압수목적달성에 어려운 점이 많다. 이에 현재의 압수수색방법의 문제점과 새로운 첨단 환경하의 디지털증거의 바람직한 현장 압수수색방법과 개선방안을 제시한다.
Amyloid proteins, which aggregate to form highly ordered structures, play a crucial role in various disease pathologies. Despite many previous studies on amyloid fibrils, which are an end product of protein aggregation, the structural characteristics of amyloid proteins in the early stage of aggregation and their related aggregation mechanism still remain elusive. The role of the amino acid sequence in the aggregation-prone structures of amyloid proteins at such a stage is not understood. Here,
We report the synthesis of surface-composition-controlled gold–platinum (AuPt) bimetallic nanostructures on carbon nanotubes by peptide-based self-assembly and their catalytic responses to oxygen reduction. Our results can provide a great opportunity to construct various nanostructures with tailored properties.
Research Areas
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