<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Rane, Sandhya</style></author><author><style face="normal" font="default" size="100%">Ahmed, Khursheed</style></author><author><style face="normal" font="default" size="100%">Salunke-Gawali, Sunita</style></author><author><style face="normal" font="default" size="100%">Zaware, Santosh B.</style></author><author><style face="normal" font="default" size="100%">Srinivas, D.</style></author><author><style face="normal" font="default" size="100%">Gonnade, Rajesh G.</style></author><author><style face="normal" font="default" size="100%">Bhadbhade, Mohan M.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Vitamin K-3 family members - Part II: Single crystal X-ray structures, temperature-induced packing polymorphism, magneto-structural correlations and probable anti-oncogenic candidature</style></title><secondary-title><style face="normal" font="default" size="100%">Journal of Molecular Structure</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Anti-oncogenic candidature</style></keyword><keyword><style  face="normal" font="default" size="100%">H-bonding</style></keyword><keyword><style  face="normal" font="default" size="100%">Magneto-structural correlations</style></keyword><keyword><style  face="normal" font="default" size="100%">Naphthosemiquinones in vitamin K-3 family</style></keyword><keyword><style  face="normal" font="default" size="100%">Packing polymorphism</style></keyword><keyword><style  face="normal" font="default" size="100%">Spin concentrations</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2008</style></year><pub-dates><date><style  face="normal" font="default" size="100%">DEC</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">1-3</style></number><publisher><style face="normal" font="default" size="100%">ELSEVIER SCIENCE BV</style></publisher><pub-location><style face="normal" font="default" size="100%">PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS</style></pub-location><volume><style face="normal" font="default" size="100%">892</style></volume><pages><style face="normal" font="default" size="100%">74-83</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Temperature-induced packing polymorphism is observed for vitamin K-3 (menadione, 3-methyl-1,4-naphthoquinone, 1). Form la crystallizes at 300 K and 1b at 277 K both in the same space group P2(1)/c. Form 1b contains one molecule per asymmetric unit, performing anisotropy in g-factor viz. g(z) = 2.0082, g(y) = 2.0055 and g(x) = 2.0025, whereas form 1a contains two molecules in its asymmetric unit. Vitamin K-3 family members 2, [2-hydroxy vitamin K-3] and 3, [2-hydroxy-1-oximino vitamin K-3] also perform intrinsic neutral active naphthosemiquinone valence tautomers even in dark having spin concentrations due to hydrogen bonding and aromatic stacking interactions which are compared to vitamin K-3. The significant lateral C-H center dot center dot center dot O and O-H center dot center dot center dot pi bifurcated or pi-pi(center dot) interactions are discussed for molecular associations and radical formations. X-ray structure of 3 revealed pi-pi(center dot) stack dimers as radicals signatured in PR as triplet with five hyperfine splits [(A) over bar(N-14) = 11.9 G]. The centrosymmetric biradicals in 3 show diamagnetism at high temperature but below 10 K it shows paramagnetism with mu(eff) as 0.19 B.M. Vitamin K-3 and its family members inhibit biological activities of acid phosphatase (APase), which are proportional to their spin concentrations. This may relate to their probable anti-oncogenic candidature in future. (C) 2008 Elsevier B.V. All rights reserved.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">1-3</style></issue><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">1.78</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Enumula, Sreenivasulu</style></author><author><style face="normal" font="default" size="100%">Shaikh, Javed</style></author><author><style face="normal" font="default" size="100%">Shaikh, Amin</style></author><author><style face="normal" font="default" size="100%">Sheikh, Kounsar N.</style></author><author><style face="normal" font="default" size="100%">Tambe, Pranav</style></author><author><style face="normal" font="default" size="100%">Lande, Dipali N.</style></author><author><style face="normal" font="default" size="100%">Gejji, Shridhar P.</style></author><author><style face="normal" font="default" size="100%">Shaligram, Parth</style></author><author><style face="normal" font="default" size="100%">Gonnade, Rajesh</style></author><author><style face="normal" font="default" size="100%">Bhadbhade, Mohan</style></author><author><style face="normal" font="default" size="100%">Ahmed, Khursheed</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Structural characterisation, anticancer properties, and BSA binding of 2,6-dipyrazinylpyridines: Insights from experiment and theory</style></title><secondary-title><style face="normal" font="default" size="100%">Journal of Molecular Structure</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">2</style></keyword><keyword><style  face="normal" font="default" size="100%">6-dipyrazinylpyridines</style></keyword><keyword><style  face="normal" font="default" size="100%">Bovine serum albumin interaction</style></keyword><keyword><style  face="normal" font="default" size="100%">Cytotoxicity (HCT-116 cells)</style></keyword><keyword><style  face="normal" font="default" size="100%">Density functional theory</style></keyword><keyword><style  face="normal" font="default" size="100%">Halogenated derivatives</style></keyword><keyword><style  face="normal" font="default" size="100%">Single-crystal X-ray diffraction</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2026</style></year><pub-dates><date><style  face="normal" font="default" size="100%">FEB </style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">1351</style></volume><pages><style face="normal" font="default" size="100%">144225</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;
	The phenyl-(2,6-di-2-pyrazinyl)pyridine derivatives (L1, L2) were synthesized using a one-pot Krohnke-type method, starting from 2-acetylpyrazine and substituted benzaldehydes. Their structures were characterized using a combination of spectroscopic (NMR, HRMS) and single-crystal X-ray diffraction techniques, complemented by density functional theory (DFT). Single-crystal X-ray diffraction reveals that L1 crystallizes in the C2/c space group (T = 296 K) with its supramolecular assembly being stabilized by C-H &amp;amp; ctdot;N and pi-pi stacking interactions, whereas L2 facilitates C-H &amp;amp; ctdot;N, N-H &amp;amp; ctdot;pi bifurcated, and pi-pi* interactions. The bio-interaction properties of L1 were studied using fluorescence spectroscopy with bovine serum albumin (BSA) as a model protein. Fluorescence studies demonstrated L1 induces static quenching of BSA, with a binding constant of 5.15 x 104 mol &amp;amp; sdot;dm-3. Synchronous and three-dimensional fluorescence spectra further demonstrated that L1 brings forth significant conformational changes in BSA. The compounds were evaluated for cytotoxicity against the HCT-116 human colorectal cancer cell line.&lt;/p&gt;
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	Foreign&lt;/p&gt;
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