PMID- 27345944
OWN - NLM
STAT- MEDLINE
DCOM- 20170724
LR  - 20180208
IS  - 1742-2051 (Electronic)
IS  - 1742-2051 (Linking)
VI  - 12
IP  - 9
DP  - 2016 Aug 16
TI  - Cell cytotoxicity and serum albumin binding capacity of the morin-Cu(ii) complex 
      and its effect on deoxyribonucleic acid.
PG  - 2818-33
LID - 10.1039/c6mb00344c [doi]
AB  - The dietary components, flavonoids, are important for their anti-oxidant 
      properties and the ability to act as metal ion chelators. The characterization of 
      the morin-Cu(ii) complex is executed using elemental analysis, FTIR and mass 
      spectroscopy. DNA cleaving and cell cytotoxicity properties followed by serum 
      albumin binding have been investigated in this report. The morin-Cu(ii) complex 
      was found to cleave plasmid pBR322 DNA via an oxidative pathway as revealed by 
      agarose gel based assay performed in the presence of some scavengers and reactive 
      oxygen species. The breaking of the deoxyribose ring of calf thymus DNA (ct-DNA) 
      was also confirmed by the formation of thiobarbituric acid reacting species 
      (TBARS) between thiobarbituric acid and malonaldehyde. The morin-Cu(ii) complex 
      is able to inhibit the growth of human HeLa cells. Fluorescence studies revealed 
      that the morin-Cu(ii) complex can quench the intrinsic fluorescence of serum 
      albumins (SAs) via a static quenching method. The binding constants were found to 
      be in the order of 10(5) M(-1) and observed to increase with temperature. Both 
      DeltaH degrees  and DeltaS degrees  are positive for the binding of the morin-Cu(ii) complex with serum 
      albumins which indicated the presence of hydrophobic forces. Site-selectivity 
      studies reveal that the morin-Cu(ii) complex binds to both site 1 (subdomain IIA) 
      and site 2 (subdomain IIIA) of human serum albumin (HSA) and bovine serum albumin 
      (BSA). Circular dichroism (CD) studies showed the structural perturbation of SAs 
      during binding with the morin-Cu(ii) complex. The results from binding studies 
      confirmed that after complexation with the Cu(ii) ion, morin alters its mode of 
      interaction with SAs which could have differential implications on its other 
      biological and pharmaceutical properties.
FAU - Roy, Atanu Singha
AU  - Roy AS
AD  - Department of Chemistry, Indian Institute of Technology, Kharagpur 721302, India. 
      singharoyatanu@gmail.com asroy86@nitm.ac.in.
FAU - Samanta, Sintu Kumar
AU  - Samanta SK
AD  - Department of Biotechnology, Indian Institute of Technology, Kharagpur 721302, 
      India.
FAU - Ghosh, Pooja
AU  - Ghosh P
AD  - Department of Chemistry, Indian Institute of Technology, Kharagpur 721302, India. 
      singharoyatanu@gmail.com asroy86@nitm.ac.in.
FAU - Tripathy, Debi Ranjan
AU  - Tripathy DR
AD  - Department of Chemistry, Indian Institute of Technology, Kharagpur 721302, India. 
      singharoyatanu@gmail.com asroy86@nitm.ac.in.
FAU - Ghosh, Sudip Kumar
AU  - Ghosh SK
AD  - Department of Biotechnology, Indian Institute of Technology, Kharagpur 721302, 
      India.
FAU - Dasgupta, Swagata
AU  - Dasgupta S
AD  - Department of Chemistry, Indian Institute of Technology, Kharagpur 721302, India. 
      singharoyatanu@gmail.com asroy86@nitm.ac.in.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Mol Biosyst
JT  - Molecular bioSystems
JID - 101251620
RN  - 0 (Flavonoids)
RN  - 0 (Serum Albumin)
RN  - 789U1901C5 (Copper)
RN  - 8NFQ3F76WR (morin)
RN  - 9007-49-2 (DNA)
SB  - IM
MH  - Animals
MH  - Cattle
MH  - Cell Line
MH  - Circular Dichroism
MH  - *Copper/chemistry
MH  - DNA/chemistry/*metabolism
MH  - DNA Damage
MH  - Dose-Response Relationship, Drug
MH  - Flavonoids/chemistry/*metabolism/*toxicity
MH  - Fluorescence Resonance Energy Transfer
MH  - Humans
MH  - Molecular Structure
MH  - Oxidative Stress
MH  - Protein Binding
MH  - Serum Albumin/chemistry/*metabolism
MH  - Spectrum Analysis
EDAT- 2016/06/28 06:00
MHDA- 2017/07/25 06:00
CRDT- 2016/06/28 06:00
PHST- 2016/06/28 06:00 [entrez]
PHST- 2016/06/28 06:00 [pubmed]
PHST- 2017/07/25 06:00 [medline]
AID - 10.1039/c6mb00344c [doi]
PST - ppublish
SO  - Mol Biosyst. 2016 Aug 16;12(9):2818-33. doi: 10.1039/c6mb00344c.