Insights into the binding of thiosemicarbazone derivatives with human serum albumin: spectroscopy and molecular modelling studies. Issue 6 (2nd June 2016)

• Record Type: Journal Article
• Authors: Karthikeyan, Subramani; Bharanidharan, Ganesan; Kesherwani, Manish; Mani, Karthik Ananth; Srinivasan, Narasimhan; Velmurugan, Devadasan; Aruna, Prakasarao; Ganesan, Singaravelu
• Is Part Of: Journal of biomolecular structure & dynamics. Volume 34:Issue 6(2016)
• Page Start: 1264
• Page End: 1281
• Publication Date: 2016-06-02
• Subjects: anticancer -- drug-binding pocket -- florescence resonance energy transfer -- molecular modelling; Biomolecules -- Periodicals; Molecular structure -- Periodicals; Molecular Biology -- Periodicals; Biomechanics -- Periodicals; 572
• DOI: 10.1080/07391102.2015.1075905
• Languages: English
• ISSNs: 0739-1102

Abstract

Abstract : 4-[(1 Z )-1-(2-carbamothioylhydrazinylidene)ethyl]phenyl acetate [Ace semi], 4-[(1 Z )-1-(2-carbamothioylhydrazinylidene)ethyl]phenyl propanoate [Pro semi] from the family of thiosemicarbazones derivative has been newly synthesized. It has good anticancer activity as well as antibacterial and it is also less toxic in nature, its binding characteristics are therefore of huge interest for understanding pharmacokinetic mechanism of the drug. The binding of thiosemicarbazone derivative to human serum albumin (HSA) has been investigated by studying its quenching mechanism, binding kinetics and the molecular distance ( r ) between donor (HSA) and acceptor (thiosemicarbazone derivative) was estimated according to Forster's theory of non-radiative energy transfer using fluorescence spectroscopy. The binding dynamics has been elaborated using synchronous fluorescence spectroscopy, and the feature of thiosemicarbazone derivative induced structural changes of HSA has been studied by circular dichorism, Fourier transform infrared spectroscopy. Molecular modelling simulations explore the hydrophobic interaction and hydrogen bonding which stabilizes the interaction.