PMID- 33525995
OWN - NLM
STAT- MEDLINE
DCOM- 20220721
LR  - 20220830
IS  - 1538-0254 (Electronic)
IS  - 0739-1102 (Linking)
VI  - 40
IP  - 13
DP  - 2022 Aug
TI  - Insight into the binding mechanism of macrolide antibiotic; erythromycin to calf 
      thymus DNA by multispectroscopic and computational approaches.
PG  - 6171-6182
LID - 10.1080/07391102.2021.1877821 [doi]
AB  - In the present study, the interactions between Erythromycin drug and calf thymus 
      deoxyribonucleic acid (ct-DNA) were explored by multi spectroscopic techniques 
      (UV-Visible, fluorescence, circular dichroism spectroscopies), viscosity, 
      molecular docking simulation, and atomic force microscopy (AFM). In addition, the 
      values of binding constant were calculated by the UV-Visible and fluorescence 
      spectroscopy. Competitive fluorescence study with methylene blue (MB), acridine 
      orange (AO), and Hoechst 33258 were indicated that the Erythromycin drug could 
      displace the DNA-bound Hoechst, which displays the strong competition of 
      Erythromycin with Hoechst to interact with the groove binding site of DNA. In 
      addition, the observed complexes in AFM analysis comprise the chains of ct-DNA 
      and Erythromycin with an average size of 314.05 nm. The results of thermodynamic 
      parameter calculations (DeltaS degrees  = -332.103 +/- 14 J mol(-1) K(-1) and DeltaH degrees  = 
      -115.839 +/- 0.02 kJ mol(-1)) approved the critical role of van der Waals forces 
      and hydrogen bonds in the complexation of Erythromycin-DNA. Fluorescence 
      spectroscopy results demonstrate the existence of a static enhancement mechanism 
      in the interaction of Erythromycin-DNA. According to the obtained results, 
      Erythromycin drug interacts with the major groove of ct-DNA. These consequences 
      were further supported by the molecular docking study, and it could be determined 
      that DNA-Erythromycin docked model was in a rough correlation with our 
      experimental results.Communicated by Ramaswamy H. Sarma.
FAU - Shahabadi, Nahid
AU  - Shahabadi N
AD  - Department of Inorganic Chemistry, Faculty of Chemistry, Razi University, 
      Kermanshah, Iran.
AD  - Medical Biology Research Center (MBRC), Kermanshah University of Medical 
      Sciences, Kermanshah, Iran.
FAU - Razlansari, Mahtab
AU  - Razlansari M
AD  - Department of Inorganic Chemistry, Faculty of Chemistry, Razi University, 
      Kermanshah, Iran.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20210202
PL  - England
TA  - J Biomol Struct Dyn
JT  - Journal of biomolecular structure & dynamics
JID - 8404176
RN  - 0 (Anti-Bacterial Agents)
RN  - 0 (Macrolides)
RN  - 63937KV33D (Erythromycin)
RN  - 9007-49-2 (DNA)
RN  - 91080-16-9 (calf thymus DNA)
SB  - IM
MH  - Anti-Bacterial Agents/pharmacology
MH  - Binding Sites
MH  - Circular Dichroism
MH  - *DNA/chemistry
MH  - *Erythromycin
MH  - Macrolides
MH  - Molecular Docking Simulation
MH  - Spectrometry, Fluorescence
MH  - Spectrophotometry, Ultraviolet
MH  - Thermodynamics
OTO - NOTNLM
OT  - DNA binding
OT  - Erythromycin
OT  - atomic force microscopy
OT  - fluorescence analysis
OT  - molecular docking
EDAT- 2021/02/03 06:00
MHDA- 2022/07/22 06:00
CRDT- 2021/02/02 05:41
PHST- 2021/02/03 06:00 [pubmed]
PHST- 2022/07/22 06:00 [medline]
PHST- 2021/02/02 05:41 [entrez]
AID - 10.1080/07391102.2021.1877821 [doi]
PST - ppublish
SO  - J Biomol Struct Dyn. 2022 Aug;40(13):6171-6182. doi: 
      10.1080/07391102.2021.1877821. Epub 2021 Feb 2.