https://scholar.dgist.ac.kr/handle/20.500.11750/741 2026-04-04T12:10:14Z https://scholar.dgist.ac.kr/handle/20.500.11750/60155 Title: 코로나바이러스 감염증 COVID-19 치료용 펩타이드 및 이의 용도 Author(s): 이영호; 김민기; 권욱봉; 서소욱; 박송; 민가희; 이주환; 지상호; 장익수; 김상열; 유우경; 김효은; 최재석; 김희연; 박성준; 추효섭; 오명원; 이애리; 강무석; 이경은; 최성균; 최민지 Abstract: The present invention relates to a peptide for treatment of the corona virus infection COVID-19 and a use thereof. In order to make the binding to the new epitope of SARS-CoV2 RBD stronger compared to the peptide (P6) simulating the conventionally known binding site between SARS-CoV RBD and ACE2, the peptide of the present invention includes a new portion added with a novel amino acid sequence fundamentally designed for interaction in the dimension of atoms consisting of the amino acids. Suggested in the present invention is a novel design of a peptide having higher binding affinity than conventionally known peptides, wherein an expanded peptide is creatively designed to additionally interact with charged amino acids of D420 and K458, located at the rear side of the known binding boundary between RBD and hACE2. The peptide of the present invention exhibits high possibility as a therapeutic agent for COVID-19. https://scholar.dgist.ac.kr/handle/20.500.11750/60085 Title: Effect of JIN-A02, a Novel 4Th-Generation EGFR-TKI, on Multiple EGFR Mutations in Comparison With 3Rd-Generation EGFR-TKIs Author(s): Lim, S- M.; Kim, Beom Soo; Yu, Wookyung; Choi, Seong-Kyoon; Jo, A.; Seah, E.; Kim, C.; Han, S.; Cho, B. C.; Kim, Hee-Yeon Abstract: JIN-A02, a novel fourth-generation tyrosine kinase inhibitor (TKI) targeting the epidermal growth factor receptor (EGFR) C797S mutation, is currently undergoing phase 1/2 clinical trials in patients with EGFR-mutated non-small cell lung cancer (NSCLC) in Korea, the USA, and Thailand (NCT05394831). NSCLC patients harboring acquired EGFR C797S mutations often exhibit co-occurring mutations, such as exon 19 deletions or T790M, as a result of targeted therapies, leading to tumor tissue heterogeneity. This heterogeneity significantly limits therapeutic options for these patients. To address this challenge, there is an unmet need for the development of fourth-generation EGFR-TKIs capable of targeting multiple EGFR mutations and effectively suppressing heterogeneous tumor tissues. With a view to evaluating the activity of JIN-A02 against common EGFR mutations (including T790M), we conducted an in silico study to estimate its binding affinity compared with third-generation EGFR-TKIs along with an in vitro study to calculate its inhibitory concentration (IC90) in EGFR-mutated cell lines. 2025-09-07T15:00:00Z https://scholar.dgist.ac.kr/handle/20.500.11750/59909 Title: Erythropoietin-derived Non-erythropoietic Peptides Conferring Oxidative Stress Resistance to Keratinocytes and Fibroblasts Author(s): Han, Min Ae; Ashim, Janbolat; Ji, Youngheum; Kang, Eunho; Jeong, Minchan; Kim, Sung Jae; Yu, Wookyung; Kim, Jin Hae; Moon, Cheil; Lee, Chang-Hun Abstract: Erythropoietin (EPO) exerts tissue-protective effects; however, its erythropoietic activity limits broader use. Three EPO-derived peptides (ML1-C1/C2/C3) were designed from the C-helix of EPO to remove erythropoietic activity while retaining cell-protective activity. Circular dichroism and nuclear magnetic resonance spectroscopies were used to assess the solution structures of ML1-C1/C2/C3 peptides. The peptide activities for cytoprotection and growth support were assessed using skin-relevant cells, HaCaT cells and 3T3-L1 cells, which proposes an effect on skin epithelial keratinocytes and pre-adipocytic fibroblasts, respectively. Also, an erythroid-precursor cell line, TF-1, was used to evaluate the erythropoietic function of the three peptides. Spectroscopic analyses of ML1-C1/C2/C3 peptides revealed similar secondary structures and different flexibilities between the peptides. While ML1-C1 and ML1-C3 had highly flexible loop-like structures, ML1-C2 had less flexible loop-like structures. Also, their cellular effects vary in a cell type-dependent manner. The EPO-derived peptides can attenuate H2O2-induced loss of viability in HaCaT cells and 3T3-L1 cells. Under low-serum conditions, the three peptides promoted HaCaT proliferation, whereas only ML1-C1 improved 3T3-L1 proliferation. In TF-1 cells, none of the peptides increased cell viability or hemoglobin staining, whereas recombinant human EPO did, indicating the lack of erythropoietic activity of the peptides under experimental conditions. These findings support the potential of EPO-derived peptides as skin-protective agents and motivate future work for skin therapeutics or cosmetic purposes. https://scholar.dgist.ac.kr/handle/20.500.11750/59037 Title: The N-terminal order-disorder transition is a critical determinant for a metamorphosis of IscU Author(s): Na, Jongbum; Heo, Joongyu; Jeong, Minchan; Kim, Beom Soo; Ji, Sangho; Ko, Young Ho; Shafiei, Alaleh; Baldir, Nilufer; DeMirci, Hasan; Yu, Wookyung; Kim, Jin Hae Abstract: IscU, a key scaffold protein mediating the biogenesis of iron‑sulfur (Fesingle bondS) clusters, exhibits metamorphic characteristics crucial for its versatile and efficient function. Previous studies have demonstrated that IscU has two interconverting conformations: the structured state (S-state) and the disordered state (D-state), each contributing to its distinct functionality and interaction network. Despite its physiological importance, the precise mechanism underpinning the maintenance of IscU's unique structural heterogeneity has remained elusive. In this study, we used computational, spectroscopic, and biochemical approaches to reveal that the N-terminal order-disorder plays a critical role in the metamorphic modulation of Escherichia coli IscU. With computational analysis, we found that the N-terminal region displays greater structural plasticity, which is linked to other regions of IscU through coevolutionary relationships. We also used site-directed mutagenesis, size-exclusion chromatography, circular dichroism, isothermal titration calorimetry, and nuclear magnetic resonance spectroscopic techniques to demonstrate that the degree of orderliness in the N-terminal region correlates positively with the stabilization of IscU's S-state and negatively with its affinity for HscA. Finally, we also showed that the peptide mimicking the N-terminal motif can modulate IscU's metamorphic properties. Our data indicate that the flexibility in the N-terminal region is finely tuned to optimize IscU's physiological efficiency and efficacy. Moreover, our study showcases important evidence suggesting a novel therapeutic potential of the N-terminus-like peptide for related pathogenic processes. 2025-08-31T15:00:00Z