• Title/Summary/Keyword: Hydrophobic gating

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Development of pH-Responsive Core-Shell Microcapsule Reactor

  • Akamatsu, Kazuki;Yamaguchi, Takeo
    • Proceedings of the Membrane Society of Korea Conference
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    • 2004.05a
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    • pp.191-194
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    • 2004
  • A novel type of intelligent microcapsule reactor system was prepared. The reactor can recognize pH change in the medea and control reaction rate by itself. For the reactor system, acrylic acid (AA), N-isopropylacrylamide (NIPAM), and glucose oxidase (GOD) were selected as a pH-responsive device, a gating device according and a reaction device, respectively. Poly(NIPAM-co-AA) (P-NIPAM-co-AA) are known to change its hydrophilicity-hydrophobicity due to pH change. They were integrated in a core-shell microcapsule space. GOD was loaded inside the core space and the pores in the outside shell layer were filled with P-NIPAM-co-AA linear grafted chains as pH-responsive gates by plasma graft filling polymerization method. When P-NIPAM-co-AA gates are hydrophilic at high pH value, this microcapsule permits glucose penetration into the core space and GOD reaction proceeds. However, when P-NIPAM-co-AA gates are hydrophobic at low pH value, this microcapsule forbids glucose penetration and GOD reaction will not occur. The accuracy of this concept was examined.

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Electrochemical Mass Transport Control in Biomimetic Solid-State Nanopores (생체모사형 나노포어를 활용한 전기화학 기반 물질전달 조절 시스템)

  • Soongyu Han;Yerin Bang;Joon-Hwa Lee;Seung-Ryong Kwon
    • Journal of the Korean Electrochemical Society
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    • v.26 no.4
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    • pp.43-55
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    • 2023
  • Mass transport through nanoporous structures such as nanopores or nanochannels has fundamental electrochemical implications and many potential applications as well. These structures can be particularly useful for water treatment, energy conversion, biosensing, and controlled delivery of substances. Earlier research focused on creating nanopores with diameters ranging from tens to hundreds of nanometers that can selectively transport cationic or anionic charged species. However, recent studies have shown that nanopores with diameters of a few nanometers or even less can achieve more complex and versatile transport control. For example, nanopores that mimic biological channels can be functionalized with specific receptors to detect viruses, small molecules, and even ions, or can be made hydrophobic and responsive to external stimuli, such as light and electric field, to act as efficient valves. This review summarizes the latest developments in nanopore-based systems that can control mass transport based on the size of the nanopores (e.g., length, diameter, and shape) and the physical/chemical properties of their inner surfaces. It also provides some examples of practical applications of these systems.

Ribosomal Crystallography: Peptide Bond Formation, Chaperone Assistance and Antibiotics Activity

  • Yonath, Ada
    • Molecules and Cells
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    • v.20 no.1
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    • pp.1-16
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    • 2005
  • The peptidyl transferase center (PTC) is located in a protein free environment, thus confirming that the ribosome is a ribozyme. This arched void has dimensions suitable for accommodating the 3'ends of the A-and the P-site tRNAs, and is situated within a universal sizable symmetry-related region that connects all ribosomal functional centers involved in amino-acid polymerization. The linkage between the elaborate PTC architecture and the A-site tRNA position revealed that the A-to P-site passage of the tRNA 3'end is performed by a rotatory motion, which leads to stereochemistry suitable for peptide bond formation and for substrate mediated catalysis, thus suggesting that the PTC evolved by genefusion. Adjacent to the PTC is the entrance of the protein exit tunnel, shown to play active roles in sequence-specific gating of nascent chains and in responding to cellular signals. This tunnel also provides a site that may be exploited for local co-translational folding and seems to assist in nascent chain trafficking into the hydrophobic space formed by the first bacterial chaperone, the trigger factor. Many antibiotics target ribosomes. Although the ribosome is highly conserved, subtle sequence and/or conformational variations enable drug selectivity, thus facilitating clinical usage. Comparisons of high-resolution structures of complexes of antibiotics bound to ribosomes from eubacteria resembling pathogens, to an archaeon that shares properties with eukaryotes and to its mutant that allows antibiotics binding, demonstrated the unambiguous difference between mere binding and therapeutical effectiveness. The observed variability in antibiotics inhibitory modes, accompanied by the elucidation of the structural basis to antibiotics mechanism justifies expectations for structural based improved properties of existing compounds as well as for the development of novel drugs.