Publications by authors named "Yeongseon Jang"

Article Synopsis
  • - Sensory capabilities are essential for cellular interaction, leading to the development of sensory globular protein vesicles (GPVs) made from recombinant fusion proteins that self-assemble in water.
  • - GPVs functionally interact with the signaling molecule rapamycin to form a FKBP-FRB ternary complex, which incorporates a genetically fused fluorescent protein and leucine zipper for vesicle assembly.
  • - The study reveals that GPVs can aggregate in response to rapamycin in a time- and concentration-dependent way, providing insights into their potential use as models for mimicking key cellular processes in synthetic biology.
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We present a straightforward strategy for constructing giant, multicompartmentalized vesicles using recombinant fusion proteins. Our method leverages the self-assembly of globule-zipper-elastin-like polypeptide fusion protein complexes in aqueous conditions, eliminating the need for organic solvents and chemical conjugation. By employing the thin-film rehydration method, we have successfully encapsulated a diverse range of bioactive macromolecules and engineered organelle-like compartments─ranging from soluble proteins and coacervate droplets to vesicles─within these protein-assembled giant vesicles.

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Bioluminescence is a type of chemiluminescence that arises from a luciferase-catalyzed oxidation reaction of luciferin. Molecular biology and comparative genomics have recently elucidated the genes involved in fungal bioluminescence and the evolutionary history of their clusters. However, most studies on fungal bioluminescence have been limited to observing the changes in light intensity under various conditions.

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(Sarcoscyphaceae, Pezizales) is a saprobic fungus characterized by the cup or disc-shaped blight red apothecium and oblong to ellipsoid ascospores. The 18 species of were known to occur in Europe, North America, and tropical Asia. However, up to date, only two species have been reported in Korea.

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Synthetic cells are artificial constructs that mimic the structures and functions of living cells. They are attractive for studying diverse biochemical processes and elucidating the origins of life. While creating a living synthetic cell remains a grand challenge, researchers have successfully synthesized hundreds of unique synthetic cell platforms.

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Protein nanoparticles are promising targeted drug delivery carriers due to their low toxicity, biodegradability, and abundance of proteins in natural sources. Also, protein nanoparticles enable surface modification with other functional proteins or carbohydrate ligands, which improves the efficacy of targeted drug delivery. Nonetheless, a persistent challenge remains to make versatile protein nanoparticles that deliver diverse types of drugs in a wide range of water solubility.

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Synthetic vesicles have gained considerable popularity in recent years for numerous biological and medical applications. Among the various types of synthetic vesicles, the utilization of polypeptides and/or proteins as fundamental constituents has garnered significant interest for vesicle construction owing to the unique bio-functionalities inherent in rationally designed amino acid sequences. Especially the incorporation of functional proteins onto the vesicle surface facilitates a wide range of advanced biological applications that are not easily attainable with traditional building blocks, such as lipids and polymers.

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In this study, we investigate the changes in the permeability of the recombinant fusion protein vesicles with different membrane structures as a function of solution temperature. The protein vesicles are self-assembled from recombinant fusion protein complexes composed of an mCherry fused with a glutamic acid-rich leucine zipper and a counter arginine-rich leucine zipper fused with an elastin-like polypeptide (ELP). We have found that the molecular weight cut-off (MWCO) of the protein vesicle membranes varies inversely with solution temperature by monitoring the transport of fluorescent-tagged dextran dyes with different molecular weights.

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The diversity of mating type in wild strains of was extensively analyzed to characterize and utilize them for developing new cultivars. One hundred twenty-three mating type alleles, including 67 newly discovered alleles, were identified from 106 wild strains collected for the past four decades in Korea. Based on previous studies and current findings, a total of 130  mating type alleles have been found, 124 of which were discovered from wild strains, indicating the hyper-variability of mating type alleles of .

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Article Synopsis
  • Porous membranes are essential in in vitro cell coculture systems as they mimic the in vivo environment, allowing for communication between different cell types.
  • Conventional systems like Transwell® have limitations in controlling cell interactions and separation during implantation.
  • The design of advanced coculture platforms is driven by the need to optimize pore size, number, and membrane thickness to enhance cell signaling and overall performance in heterogeneous cultures.
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The desire to develop artificial cells to imitate living cells in synthetic vesicle platforms has continuously increased over the past few decades. In particular, heterogeneous synthetic vesicles made from two or more building blocks have attracted attention for artificial cell applications based on their multifunctional modules with asymmetric structures. In addition to the traditional liposomes or polymersomes, polypeptides and proteins have recently been highlighted as potential building blocks to construct artificial cells owing to their specific biological functionalities.

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Antimicrobial resistance is one of the greatest global threats. Particularly, multidrug resistant extended-spectrum β-lactamase (ESBL)-producing pathogens confer resistance to many commonly used medically important antibiotics, especially beta-lactam antibiotics. Here, we developed an innovative combination approach to therapy for multidrug resistant pathogens by encapsulating cephalosporin antibiotics and β-lactamase inhibitors with chitosan nanoparticles (CNAIs).

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Species of Arthrinium are well-known plant pathogens, endophytes, or saprobes found in various terrestrial habitats. Although several species have been isolated from marine environments and their remarkable biological activities have been reported, marine Arthrinium species remain poorly understood. In this study, the diversity of this group was evaluated based on material from Korea, using morphological characterization and molecular analyses with the internal transcribed spacer (ITS) region, β-tubulin (TUB), and translation elongation factor 1-alpha (TEF).

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Vesicles made from functionally folded, globular proteins that perform specific biological activities, such as catalysis, sensing, or therapeutics, show potential applications as artificial cells, microbioreactors, or protein drug delivery vehicles. The mechanical properties of vesicle membranes, including the elastic modulus and hardness, play a critical role in dictating the stability and shape transformation of the vesicles under external stimuli triggers. Herein, we have developed a strategy to tune the mechanical properties and integrity of globular protein vesicle (GPV) membranes of which building molecules are recombinant fusion protein complexes: a mCherry fused with an acidic leucine zipper (mCherry-Z) and a basic leucine zipper fused with an elastin-like polypeptide (Z-ELP).

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Shiga toxin-producing (STEC) are critical foodborne pathogens, which cause serious human health issues, including hemolytic uremic syndrome. Illnesses caused by STEC lack effective treatments that target the elimination of these bacteria from the gastrointestinal tract without causing an adverse effect. Reducing this pathogen from a reservoir of STEC is an effective strategy, but the challenges remain due to the lack of efficient, selective antimicrobial agents.

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The presence of excessive osteoclasts is a major factor in skeletal diseases. The present study aimed to discover osteoclast differentiation inhibitors from the basidiomycete . Seven new drimane sesquiterpenoids (-) and 7-ketoisodrimenin-5-ene () were obtained and characterized by various spectroscopic methods.

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The environmental accumulation of polycyclic aromatic hydrocarbons (PAHs) is of great concern due to potential carcinogenic and mutagenic risks, as well as their resistance to remediation. While many fungi have been reported to break down PAHs in environments, the details of gene-based metabolic pathways are not yet comprehensively understood. Specifically, the genome-scale transcriptional responses of fungal PAH degradation have rarely been reported.

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Protein-rich coacervates are liquid phases separate from the aqueous bulk phase that are used by nature for compartmentalization and more recently have been exploited by engineers for delivery and formulation applications. They also serve as an intermediate phase in an assembly path to more complex structures, such as vesicles. Recombinant fusion protein complexes made from a globular protein fused with a glutamic acid-rich leucine zipper (globule-Z) and an arginine-rich leucine zipper fused with an elastin-like polypeptide (Z-ELP) show different phases from soluble, through an intermediate coacervate phase, and finally to vesicles with increasing temperature of the aqueous solution.

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Anti-biofouling has been improved by passive or active ways. Passive antifouling strategies aim to prevent the initial adsorption of foulants, while active strategies aim to eliminate proliferative fouling by destruction of the chemical structure and inactivation of the cells. However, neither passive antifouling strategies nor active antifouling strategies can solely resist biofouling due to their inherent limitations.

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We demonstrate that the molecular structure of a synthetic homopolypeptide that resembles the leg architecture of water strider insects is effective to impart flexible polymeric surfaces with superhydrophobic behavior. Filter paper (FP) and polyester (PET) were modified with a coating consisting of low-molecular weight α-helical poly(γ-stearyl-α,l-glutamate) (PSLG, M = 4500 Da) homopolypeptide. PSLG-coated substrates displayed near to and superhydrophobic behavior (≥150°) as reflected by the contact angle values.

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The genus (Hypocreaceae, Ascomycota) consists of globally distributed fungi. Among them, , one of the most commonly collected species, had been known as a polyphyletic or aggregate species. However, a total of 19 species were determined from the polyphyletic groups of .

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Prevention of biofouling and microbial contamination of implanted biomedical devices is essential to maintain their functionality and biocompatibility. For this purpose, polypept(o)ide block copolymers have been developed, in which a protein-resistant polysarcosine (pSar) block is combined with a dopamine-modified poly(glutamic acid) block for surface coating and silver nanoparticles (Ag NPs) formation. In the development of a novel, versatile, and biocompatible antibacterial surface coating, block lengths pSar were varied to derive structure-property relationships.

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Bacterial adhesion to stainless steel 316L (SS316L), which is an alloy typically used in many medical devices and food processing equipment, can cause serious infections along with substantial healthcare costs. This work demonstrates that nanotextured SS316L surfaces produced by electrochemical etching effectively inhibit bacterial adhesion of both Gram-negative and Gram-positive , but exhibit cytocompatibility and no toxicity toward mammalian cells in vitro. Additionally, the electrochemical surface modification on SS316L results in formation of superior passive layer at the surface, improving corrosion resistance.

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Vesicles assembled from folded, globular proteins have potential for functions different from traditional lipid or polymeric vesicles. However, they also present challenges in understanding the assembly process and controlling vesicle properties. From detailed investigation of the assembly behavior of recombinant fusion proteins, this work reports a simple strategy to engineer protein vesicles containing functional, globular domains.

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