Interaction of Lysozyme with Rhodamine B: A combined analysis of spectroscopic & molecular docking.
J Photochem Photobiol B
; 162: 248-257, 2016 Sep.
Article
in En
| MEDLINE
| ID: mdl-27390893
ABSTRACT
The interaction of Rhodamine B (RB) with Lysozyme (Lys) was investigated by different optical spectroscopic techniques such as absorption, fluorescence, and circular-dichroism (CD), along with molecular docking studies. The fluorescence results (including steady-state and time-resolved mode) revealed that the addition of RB effectively causes strong quenching of intrinsic fluorescence in Lysozyme and mostly, by the static quenching mechanism. Different binding and thermodynamic parameters were calculated at different temperatures and the binding constant value was found to be 2963.54Lmol(-1) at 25°C. The average distance (r0) was found to be 3.31nm according to Förster's theory of non-radiative energy transfer between Lysozyme and RB. The conformational change in Lysozyme during interaction with RB was confirmed from absorbance, synchronous fluorescence, and circular dichroism measurements. Finally, molecular docking studies were done to confirm that the dye binds with Lysozyme.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Rhodamines
/
Muramidase
/
Molecular Docking Simulation
Language:
En
Journal:
J Photochem Photobiol B
Journal subject:
BIOLOGIA
Year:
2016
Document type:
Article
Affiliation country:
India