PMID- 27077554
OWN - NLM
STAT- MEDLINE
DCOM- 20170227
LR  - 20220318
IS  - 1873-2682 (Electronic)
IS  - 1011-1344 (Linking)
VI  - 159
DP  - 2016 Jun
TI  - Binding of fluorescent acridine dyes acridine orange and 9-aminoacridine to 
      hemoglobin: Elucidation of their molecular recognition by spectroscopy, 
      calorimetry and molecular modeling techniques.
PG  - 169-78
LID - S1011-1344(16)30114-2 [pii]
LID - 10.1016/j.jphotobiol.2016.03.045 [doi]
AB  - The molecular interaction between hemoglobin (HHb), the major human heme protein, 
      and the acridine dyes acridine orange (AO) and 9-aminoacridine (9AA) was studied 
      by various spectroscopic, calorimetric and molecular modeling techniques. The 
      dyes formed stable ground state complex with HHb as revealed from spectroscopic 
      data. Temperature dependent fluorescence data showed the strength of the 
      dye-protein complexation to be inversely proportional to temperature and the 
      fluorescence quenching was static in nature. The binding-induced conformational 
      change in the protein was investigated using circular dichroism, synchronous 
      fluorescence, 3D fluorescence and FTIR spectroscopy results. Circular dichroism 
      data also quantified the alpha-helicity change in hemoglobin due to the binding of 
      acridine dyes. Calorimetric studies revealed the binding to be endothermic in 
      nature for both AO and 9AA, though the latter had higher affinity, and this was 
      also observed from spectroscopic data. The binding of both dyes was entropy 
      driven. pH dependent fluorescence studies revealed the existence of electrostatic 
      interaction between the protein and dye molecules. Molecular modeling studies 
      specified the binding site and the non-covalent interactions involved in the 
      association. Overall, the results revealed that a small change in the acridine 
      chromophore leads to remarkable alteration in the structural and thermodynamic 
      aspects of binding to HHb.
CI  - Copyright (c) 2016 Elsevier B.V. All rights reserved.
FAU - Chatterjee, Sabyasachi
AU  - Chatterjee S
AD  - Biophysical Chemistry Laboratory, Organic and Medicinal Chemistry Division, 
      CSIR-Indian Institute of Chemical Biology, 4, Raja S.C. Mullick Road, Kolkata 700 
      032, India.
FAU - Kumar, Gopinatha Suresh
AU  - Kumar GS
AD  - Biophysical Chemistry Laboratory, Organic and Medicinal Chemistry Division, 
      CSIR-Indian Institute of Chemical Biology, 4, Raja S.C. Mullick Road, Kolkata 700 
      032, India. Electronic address: gskumar@iicb.res.in.
LA  - eng
PT  - Journal Article
DEP - 20160403
PL  - Switzerland
TA  - J Photochem Photobiol B
JT  - Journal of photochemistry and photobiology. B, Biology
JID - 8804966
RN  - 0 (Fluorescent Dyes)
RN  - 0 (Hemoglobins)
SB  - IM
MH  - Calorimetry
MH  - Circular Dichroism
MH  - Fluorescent Dyes/*chemistry
MH  - Hemoglobins/*chemistry
MH  - Humans
MH  - Models, Molecular
MH  - Molecular Dynamics Simulation
MH  - Spectrometry, Fluorescence
MH  - Thermodynamics
OTO - NOTNLM
OT  - Acridine dyes
OT  - Calorimetry
OT  - Dye-protein association
OT  - Molecular modeling
OT  - Spectroscopy
EDAT- 2016/04/15 06:00
MHDA- 2017/02/28 06:00
CRDT- 2016/04/15 06:00
PHST- 2016/02/26 00:00 [received]
PHST- 2016/03/29 00:00 [accepted]
PHST- 2016/04/15 06:00 [entrez]
PHST- 2016/04/15 06:00 [pubmed]
PHST- 2017/02/28 06:00 [medline]
AID - S1011-1344(16)30114-2 [pii]
AID - 10.1016/j.jphotobiol.2016.03.045 [doi]
PST - ppublish
SO  - J Photochem Photobiol B. 2016 Jun;159:169-78. doi: 
      10.1016/j.jphotobiol.2016.03.045. Epub 2016 Apr 3.