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Investigation of Optical Spectroscopic and Computational Binding Mode of Bovine Serum Albumin with 1, 4‐Bis ((4‐((4‐Heptylpiperazin‐1‐yl) Methyl)‐1 H ‐1, 2, 3‐Triazol‐1‐yl) Methyl) Benzene
Author(s) -
Karthikeyan Subramani,
Chinnathambi Shanmugavel,
Kannan Ayyavoo,
Rajakumar Perumal,
Velmurugan Devadasan,
Bharanidharan Ganesan,
Aruna Prakasarao,
Ganesan Singaravelu
Publication year - 2015
Publication title -
journal of biochemical and molecular toxicology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.526
H-Index - 58
eISSN - 1099-0461
pISSN - 1095-6670
DOI - 10.1002/jbt.21704
Subject(s) - bovine serum albumin , chemistry , serum albumin , stereochemistry , biochemistry
ABSTRACT A newly synthesized 1, 4‐bis ((4‐((4‐heptylpiperazin‐1‐yl) methyl)‐1 H ‐1, 2, 3‐triazol‐1‐yl) methyl) benzene from the family of piperazine derivative has good anticancer activity, antibacterial and low toxic nature; its binding characteristics are therefore of huge interest for understanding pharmacokinetic mechanism of the drug. The binding of piperazine derivative to bovine serum albumin (BSA) was investigated using fluorescence spectroscopy. The molecular distance r between the donor (BSA) and acceptor (piperazine derivative) was estimated according to Forster's theory of nonradiative energy transfer. The physicochemical properties of piperazine derivative, which induced structural changes in BSA, have been studied by circular dichroism and those chemical environmental changes were probed using Raman spectroscopic analysis. Further, the binding dynamics was expounded by synchronous fluorescence spectroscopy and molecular modeling studies explored the hydrophobic interaction and hydrogen bonding results, which stabilize the interaction.