Exploring the binding mechanism between methylene blue and ovalbumin using spectroscopic analyses and computational simulations

A1 Originalartikel i en vetenskaplig tidskrift (referentgranskad)

Interna författare/redaktörer

Publikationens författare: Perumal Manivel, Marimuthu Parthiban, Malaichamy Ilanchelian
Förläggare: Taylor & Francis Inc.
Publiceringsår: 2019
Tidskrift: Journal of Biomolecular Structure and Dynamics
Artikelns första sida, sidnummer: 1
Artikelns sista sida, sidnummer: 10


The detailed investigation of methylene blue (MB) dye with ovalbumin
(OVA) was examined by multispectroscopic and computational techniques.
The experimental results of emission spectral studies displayed that the
quenching behaviour of OVA with MB dye is due to static quenching
mechanism. Isothermal titration calorimetry experimental results
suggested that the binding of MB dye became favoured with the aid of a
favourable entropy contribution and negative enthalpy. The absorption
and circular dichroism spectral experiments showed that the binding of
MB dye prompted conformational modifications to the secondary structure
of OVA protein. The computational studies have been used to predict the
binding region and the stability of MB in OVA protein.

Senast uppdaterad 2020-29-03 vid 06:54