TY  - JOUR
ID  - open3232
UR  - http://crdd.osdd.net/open/3232/
IS  - 19
A1  - Kaur, Kiranjot
A1  - Sharma, Deepak
A1  - Haldar, Krishna Kanta
A1  - Kumar, Rajesh
Y1  - 2025/05//
N2  - Au/ZnO nanocomposites (NCs) were synthesized and characterized by using various analytical techniques. Analysis of Au/ZnO NCs effect on 1H NMR, CD, fluorescence, and absorbance spectra of horse myoglobin (h-Mb) at 0.0 and 5.0 M urea (pH 7.4) revealed that the Au/ZnO NCs weaken the heme-globin interactions and also disrupt the secondary/tertiary structure of h-Mb. Furthermore, the Au/ZnO NCs effect of weakening the heme-globin interactions and disrupting the protein structures was detected more in the denaturant media than in the aqueous solution. Analysis of the Au/ZnO NCs effect on thermodynamic parameters (based on absorbance at 409 nm, CD at 222 nm, and DSC) of h-Mb at pH 7.4 revealed that the Au/ZnO NCs decrease the thermodynamic stability of h-Mb. Investigation of Au/ZnO NC's effects on urea concentration-dependent unfolding free energy of h-Mb at pH 7.4 showed that the Au/ZnO NCs strengthen the urea impact to decrease the thermodynamic stability of h-Mb. The quantitative estimation of enthalpic and entropic contributions to the Au/ZnO NCs-mediated decrease in the unfolding free energy of h-Mb reveals that the Au/ZnO NCs decrease the local (heme-globin interactions) and structural thermodynamic stability of the protein due to the enthalpic interactions of h-Mb with Au/ZnO NCs. ITC and time-resolved fluorescence studies of h-Mb further suggest that the Au/ZnO NCs form binding interactions with h-Mb at pH 7.4.
PB  - American Chemical Society (ACS)
JF  - Langmuir
VL  - 41
TI  - Deciphering the underlying mechanism for Au/ZnO nanocomposites-induced modulation of structural features and thermodynamic stability of horse myoglobin
SP  - 12008
EP  - 12021
ER  -