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1.
Nanomaterials (Basel) ; 13(19)2023 Sep 22.
Article in English | MEDLINE | ID: mdl-37836263

ABSTRACT

In this paper, a new synthesis of carbon nanofibers (CNFs)/carbon nanowalls (CNWs) was performed to improve the characteristics of anode materials of lithium-ion batteries by using the advantages offered by CNWs and CNFs. Among the carbon-based nanomaterials, CNWs provide low resistance and high specific surface area. CNFs have the advantage of being stretchable and durable. The CNWs were grown using a microwave plasma-enhanced chemical vapor deposition (PECVD) system with a mixture of methane (CH4) and hydrogen (H2) gases. Polyacrylonitrile (PAN) and N,N-Dimethyl Formamide (DMF) were stirred to prepare a solution and then nanofibers were fabricated using an electrospinning method. Heat treatment in air was then performed using a hot plate for stabilization. In addition, heat treatment was performed at 800 °C for 2 h using rapid thermal annealing (RTA) to produce CNFs. A field emission scanning electron microscope (FE-SEM) was used to confirm surface and cross-sectional images of the CNFs/CNWs anode materials. Raman spectroscopy was used to examine structural characteristics and defects. Cyclic voltammetry (CV), electrochemical impedance spectroscopy (EIS), and constant current charge/discharge tests were performed to analyze the electrical characteristics. The synthesized CNFs/CNWs anode material had a CV value in which oxidation and reduction reactions were easily performed, and a low Rct value of 93 Ω was confirmed.

2.
J Med Chem ; 64(18): 13540-13550, 2021 09 23.
Article in English | MEDLINE | ID: mdl-34473495

ABSTRACT

The polyprenyl lipid undecaprenyl phosphate (C55P) is the universal carrier lipid for the biosynthesis of bacterial cell wall polymers. C55P is synthesized in its pyrophosphate form by undecaprenyl pyrophosphate synthase (UppS), an essential cis-prenyltransferase that is an attractive target for antibiotic development. We previously identified a compound (MAC-0547630) that showed promise as a novel class of inhibitor and an ability to potentiate ß-lactam antibiotics. Here, we provide a structural model for MAC-0547630's inhibition of UppS and a structural rationale for its enhanced effect on UppS from Bacillus subtilis versus Staphylococcus aureus. We also describe the synthesis of a MAC-0547630 derivative (JPD447), show that it too can potentiate ß-lactam antibiotics, and provide a structural rationale for its improved potentiation. Finally, we present an improved structural model of clomiphene's inhibition of UppS. Taken together, our data provide a foundation for structure-guided drug design of more potent UppS inhibitors in the future.


Subject(s)
Alkyl and Aryl Transferases/metabolism , Bacterial Proteins/metabolism , Enzyme Inhibitors/metabolism , Alkyl and Aryl Transferases/chemistry , Bacillus subtilis/enzymology , Bacterial Proteins/chemistry , Catalytic Domain , Crystallography, X-Ray , Enzyme Inhibitors/chemistry , Enzyme Inhibitors/pharmacology , Methicillin-Resistant Staphylococcus aureus/enzymology , Microbial Sensitivity Tests , Molecular Structure , Protein Binding , Structure-Activity Relationship
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