@article { ISI:000249329300010,
	title = {Deprotonation of 1,2-dialkylpyridinium ions: a DFT study of reactivity and site selectivity},
	journal = {Journal of Physical Chemistry A},
	volume = {111},
	number = {36},
	year = {2007},
	month = {SEP},
	pages = {8823-8828},
	publisher = {AMER CHEMICAL SOC},
	type = {Article},
	address = {1155 16TH ST, NW, WASHINGTON, DC 20036 USA},
	abstract = {<p>A site-selectivity model, based on the Fukui function as a local reactivity descriptor, has been applied to 1.2-disubstituted pyridinium ions incorporating two competing sites of similar reactivity, i.e., 1-methylene and 2-methylene, which may undergo deprotonation depending on the nature of substituent present on these moieties. Applicability of the local HSAB rule, in context with the Li-Evans{\textquoteright} generalized HSAB principle suggesting the hard-hard interactions to be controlled by minimum Fukui function, has been illustrated. Global and local reactivity descriptors have been computed by carrying out DFT calculations at B3LYP/6-31++G** level using Mulliken and NPA methods for charge analysis. A comparison with the calculated deprotonation energies involving two sites indicates that the observed site selectivity in differently substituted pyridinium ions is better explained by the Li-Evans rule of minimum Fukui function for hard-hard interactions.</p>},
	issn = {1089-5639},
	doi = {10.1021/jp072812o},
	author = {Gupta, Neelima and Garg, Reena and Shah, Kirti Kr. and Tanwar, Akhilesh and Pal, Sourav}
}
@article { ISI:000347596700001,
	title = {Molecular recognition pattern of cytotoxic alkaloid vinblastine with multiple targets},
	journal = {Journal of Molecular Graphics \& Modelling},
	volume = {54},
	year = {2014},
	month = {NOV},
	pages = {1-9},
	publisher = {ELSEVIER SCIENCE INC},
	address = {360 PARK AVE SOUTH, NEW YORK, NY 10010-1710 USA},
	abstract = {<p>Vinblastine (VLB), a cytotoxic alkaloid is used extensively against various cancer types and the crystal structure of its tubulin complex is already known. Multitarget affinity of vinblastine has been investigated and the nature of binding with biological receptors namely, duplex DNA and Human serum albumin (HSA) has been compared to the binding characteristics of its known complex with natural high affinity receptor tubulin using molecular docking and QM-MM calculations. VLB is found to interact with DNA as well as HSA protein, though, with weaker affinity as compared to tubulin. Analysis of various docked complexes revealed that the H-bonds and cation-pi bonds do not have significant contribution to the binding interactions and despite its large size, VLB remains in relaxed conformation and fits in the hydrophobic regions on the receptors. (C) 2014 Elsevier Inc. All rights reserved.</p>},
	keywords = {Drug-DNA interactions, Drug-protein binding, Human serum albumin, Molecular docking, Multitarget affinity, QM-MM calculation, Vinblastine},
	issn = {1093-3263},
	doi = {10.1016/j.jmgm.2014.09.001},
	author = {Pandya, Prateek and Agarwal, Lokesh Kr and Gupta, Neelima and Pal, Sourav}
}
