@article { ISI:000305295000014,
	title = {Design, synthesis and evaluation of unique 2,4,5-triaryl imidazole derivatives as novel potent aspartic protease inhibitors},
	journal = {Medicinal Chemistry},
	volume = {8},
	number = {3},
	year = {2012},
	month = {MAY},
	pages = {428-435},
	publisher = {BENTHAM SCIENCE PUBL LTD},
	address = {EXECUTIVE STE Y-2, PO BOX 7917, SAIF ZONE, 1200 BR SHARJAH, U ARAB EMIRATES},
	abstract = {<p>The 2,4,5-triaryl imidazole derivatives (API) were designed, screened and characterized kinetically \&amp; thermo-dynamically against Pepsin and their activity was also tested on the in silico platform. The docking studies of API with Pepsin show that these are novel and unique inhibitors of Aspartic protease. Drug like properties of these compounds were validated in silico based on Lipinski{\textquoteright}s rule of Five by calculating ClogP, LogS, H-bond acceptors, H-Bond donors, rotational bonds, PSA, PB and BBB values. The Et/Ki and Et/Km values of API show that they follow the Michaelis-Menten kinetics. The binding of inhibitors with proteases was explained by using Van{\textquoteright}t Hoff plot and thermodynamic parameters viz. free energy (Delta G), Entropy (Delta S) and Enthalpy (Delta H). The Van{\textquoteright}t Hoff analysis showed that the value of K-i decreases with increase in temperature and the binding of the inhibitor are entropically driven. API act as new potent aspartic protease inhibitors with K-i, for Pepsin, ranges from 3.7 mu M to 16.7 mu M. Strong hydrophobic groups at C-4 \&amp; C-5 position in API favor binding of inhibitors with Pepsin. Experiments also showed that among C-2 aryl substituted imidazole, a 4-substitution on aryl ring is preferred and less polar substituent makes the molecule more active whereas polar substituents at 2-position on C-2 aryl ring makes the molecule less active. The docking studies of API with Pepsin further intensify and validate our results.</p>},
	keywords = {2, 4, 5-triaryl imidazole derivatives, docking, Lipinski{\textquoteright}s rule of Five, Protease inhibitors, Thermodynamics},
	issn = {1573-4064},
	author = {Khan, Mohd Sajid and Akhtar, Salman and Siddiqui, S. A. and Siddiqui, M. S. and Srinivasan, K. V. and Arif, J. M.}
}
@article {49923,
	title = {Ready access to benzodiazocines from tryptamines: a druggable scaffold toward antiviral agents},
	journal = {ACS Medicinal Chemistry Letters},
	volume = {16},
	year = {2025},
	month = {DEC},
	pages = {2362-2367},
	type = {Article},
	abstract = {<p>
	Herein we report the first synthesis of the proposed structure of a benzodiazocine natural product, peganutonin A. Considering the druggable nature of benzodiazocine and its limited exploration in the field of medicinal chemistry, we generalized the approach and created a library of compounds useful for various biological activities. Key steps in present approach include tryptamine cyclization facilitated by tert-butyl hypochlorite and cleavage of the fused indole ring using ozonolysis. Preliminary screening of the synthesized compounds resulted in potent antiviral compounds against the SARS-CoV-2 virus.</p>
},
	keywords = {Benzodiazocine, drug discovery, Indole cleavage, Lipinski{\textquoteright}s rule of Five, SARS-CoV-2 inhibition, Tryptamine},
	issn = {1948-5875},
	doi = {10.1021/acsmedchemlett.5c00527},
	author = {Saranya, N. Sathya Sai and Choudhury, Rahul and Routholla, Ganesh and Supekar, Prathmesh R. and R, Nandhakumaar and Martin, Alna Kuriyickal and Muruganandham, Renuga Devi and Kumar, Bokara Kiran and Reddy, D. Srinivasa}
}
