

Synthesis, characterization, anticancer activity, optical spectroscopic and docking studies of novel thiophene-2-carboxaldehyde derivatives
Mohamed Ahadu Shareef (1,*)








(1) Post Graduate and Research Department of Chemistry, The New College, Chennai-600014, Tamil Nadu, India
(2) Post Graduate and Research Department of Chemistry, The New College, Chennai-600014, Tamil Nadu, India
(3) Centre of Advanced Study in Crystallography and Biophysics, University of Madras, Chennai-600025, Tamil Nadu, India
(4) Department of Medical Physics, Anna University, Chennai-600025, Tamil Nadu, India
(5) Department of Medical Physics, Anna University, Chennai-600025, Tamil Nadu, India
(6) Post Graduate and Research Department of Chemistry, Jamal Mohamed College, Tiruchirappalli-620020, Tamil Nadu, India
(7) Post Graduate and Research Department of Zoology, The New College, Chennai-600014, Tamil Nadu, India
(8) Post Graduate and Research Department of Zoology, The New College, Chennai-600014, Tamil Nadu, India
(*) Corresponding Author
Received: 31 Oct 2016 | Accepted: 19 Nov 2016 | Published: 31 Dec 2016 | Issue Date: December 2016
Abstract
2-((4-Methylpiperazin-1-yl)(thiophen-2-yl)methyl)hydrazinecarboxamide (L1) and (2-(piperazin-1-yl(thiophen-2-yl)methyl)hydrazinecarboxamide (L2) from the family of thiophene-2-carboxaldehyde derivatives have been synthesized. These new compounds have good antibacterial as well as antifungal activity and also less toxic in nature. Exemplary binding characteristics of these novel compounds and pharmacokinetic mechanism were confirmed by optical spectroscopic, anticancer and docking studies. The binding of thiophene-2-carboxaldehyde derivatives to carrier protein, Human Serum Albumin (HSA) has been investigated by studying its quenching mechanism, binding kinetics and the molecular distance (r) between donor (HSA) and acceptor (thiophene-2-carboxaldehyde derivatives) according to Forster’s theory of non-radiative energy transfer (FRET). The micro environment of HSA has also been studied by using synchronous fluorescence spectroscopy technique and the molecular docking technique has been used to explore the hydrogen bonding, hydrophobic interaction between the human serum albumin with L1 and L2 compound.
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European Journal of Chemistry
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DOI: 10.5155/eurjchem.7.4.454-462.1505
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Citations
[1]. Subramani Karthikeyan, Ganesan Bharanidharan, Sriram Ragavan, Saravanan Kandasamy, Shanmugavel Chinnathambi, Kanniyappan Udayakumar, Rajendiran Mangaiyarkarasi, Anandh Sundaramoorthy, Prakasarao Aruna, Singaravelu Ganesan
Comparative Binding Analysis of N-Acetylneuraminic Acid in Bovine Serum Albumin and Human α-1 Acid Glycoprotein
Journal of Chemical Information and Modeling 59(1), 326, 2019
DOI: 10.1021/acs.jcim.8b00558

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DOI Link: https://doi.org/10.5155/eurjchem.7.4.454-462.1505

















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