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- 저자 : Cheonik Joo (검색결과 3 건)
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Vinay K. Sharma,이기철,Cheonik Joo,Niti Sharma,정상헌 대한화학회 2011 Bulletin of the Korean Chemical Society Vol.32 No.8
To investigate the possible isosteric replacement of imidazolidinone moiety in 4-phenyl-N-arylsulfonylimidazolidinone for broad and potent anticancer agents, a series of 4-phenyl-l(N)-arylsulfonylimidazolidinones 6ak,imidazolidinethione analogs 7a-i, and imidazolidine oxime analogs 8a-c were prepared and evaluated for their in vitro anticancer activity against four human cancer cell lines (human lung A549, human colon COLO205, human leukemia K562, human ovary SK-OV-3). Among all the derivatives of N-arylsulfonylimidazolidinone 6a-k, compounds 6f and 6g showed the best inhibition comparable to doxorubicin against all cancer cell lines. Increasing the carbon chain on alkyl moieties of carbamates as shown in 6c-g did not alter the activity. The imidazolidinethione analogs 7a-i and imidazolidin-2-one oxime derivatives 8a-c did not possess any good activity. Therefore, imidazolidinone moiety is the best pharmacophore among the 4-phenyl-Narylsulfonylimidazolidinone derivatives.
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Infrared Probing of 4-Azidoproline Conformations Modulated by Azido Configurations
Lee, Kyung-Koo,Park, Kwang-Hee,Joo, Cheonik,Kwon, Hyeok-Jun,Jeon, Jonggu,Jung, Hyeon-Il,Park, Sungnam,Han, Hogyu,Cho, Minhaeng American Chemical Society 2012 The journal of physical chemistry. B, Condensed ma Vol.116 No.17
<P>4-Azidoproline (Azp) can tune the stability of the polyproline II (P<SUB>II</SUB>) conformation in collagen. The azido group in the 4<I>R</I> and 4<I>S</I> configurations stabilizes and destabilizes the P<SUB>II</SUB> conformation, respectively. To obtain insights into the dependence of the conformational stability on the azido configuration, we carried out Fourier transform (FT) IR experiments with four 4-azidoproline derivatives, Ac-(4<I>R</I>/<I>S</I>)-Azp-(NH/O)Me. We found that the amide I and azido IR spectra are different depending on the azido configuration and C-terminal structure. The origin of such spectral differences between 4<I>R</I> and 4<I>S</I> configurations and between C-terminal methylamide and ester ends was elucidated by quantum chemistry calculations in combination with <SUP>1</SUP>H NMR and time- and frequency-resolved IR pump–probe spectroscopy. We found that the azido configurations and C-terminal structures affect intramolecular interactions, which are responsible for the ensuing conformational and thereby IR spectral differences. Consequently, 4-azidoproline conformations modulated by azido configurations can be probed by IR spectroscopy. These findings suggest that 4-azidoproline can be both a structure-control and -probing element, which enables the infrared tracking of proline roles in protein structure, function, and dynamics.</P><P><B>Graphic Abstract</B> <IMG SRC='http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jpcbfk/2012/jpcbfk.2012.116.issue-17/jp1085119/production/images/medium/jp-2010-085119_0015.gif'></P><P><A href='http://pubs.acs.org/doi/suppl/10.1021/jp1085119'>ACS Electronic Supporting Info</A></P>
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Lee, Kyung-Koo,Oh, Kwang-Im,Lee, Hochan,Joo, Cheonik,Han, Hogyu,Cho, Minhaeng WILEY-VCH Verlag 2007 CHEMPHYSCHEM -WEINHEIM- Vol.8 No.15
<P>The solution structure and the local solvation environments of alanine dipeptide (AD, 1 a) and its isotopomer (AD*, 1 b, <SUP>13</SUP>C on the acetyl end C&n.dbond;O) are studied by using infrared (IR) spectroscopy and vibrational circular dichroism (VCD). From the amide I IR spectra of AD* in various protic solvents, it is found that each of the two carbonyl groups is fully H-bonded to two water molecules. However, the number of alcohol molecules H-bonded to each C&n.dbond;O varies from one to two, and the local solvation environments are asymmetric around the two peptides of AD* in alcohol solutions. The amide I VCD spectra of AD and AD* in D<SUB>2</SUB>O are also measured, and a series of density functional theory (DFT, B3LYP/6-311++G**) calculations are performed to obtain the amide I normal-mode rotational strengths of AD and the intrinsic rotational strengths of its two peptide fragments. By combining the VCD-measurement and DFT-calculation results and employing a coupled oscillator theory, we show that the aqueous-solution structure of the dipeptide can be determined. We believe that the present method will be of use in building up a library of dipeptide solution structures in water.</P> <B>Graphic Abstract</B> <P>Protein vibrations: Combined experimental studies and theoretical calculations determine the solution structure and the local solvation environments of alanine dipeptide (AD, see P<SUB>II</SUB> conformation in the figure) and its isotopomer (AD*). <img src='wiley_img/14394235-2007-8-15-CPHC200700352-content.gif' alt='wiley_img/14394235-2007-8-15-CPHC200700352-content'> </P>
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