TY - JOUR
T1 - Insight into the binding and conformational changes of hemoglobin/lysozyme with bimetallic alloy nanoparticles using various spectroscopic approaches
AU - Shanmugaraj, Krishnamoorthy
AU - Sharma, Arumugam Selva
AU - Sasikumar, Thangarasu
AU - Mangalaraja, Ramalinga Viswanathan
AU - Ilanchelian, Malaichamy
N1 - Publisher Copyright:
© 2019 Elsevier B.V.
PY - 2020/2/15
Y1 - 2020/2/15
N2 - This study explores the adsorption and binding interaction of bovine hemoglobin (BHb) and lysozyme (Lys) with gold/silver alloy nanoparticles (Au/Ag alloy NPs) using various spectroscopic approaches. The fluorescence behaviour of tryptophan residues of the proteins after Au/Ag alloy NPs addition revealed that the static quenching interactions. The changes in the morphology of Au/Ag alloy NPs upon BHb/Lys addition are characterized by HR-TEM analysis. Further, the conjugation of BHb/Lys with Au/Ag alloy NPs is evident from zeta potential and dynamic light scattering (DLS) techniques. The absorption profiles of Au/Ag alloy NPs with BHb/Lys resulted in the shift to the longer wavelength of surface plasmon resonance (SPR) band indicating the changes of refractive index around the NPs surface due to the proteins adsorption. The alteration in the structure of proteins with Au/Ag alloy NPs is evaluated using Fourier-transform infrared (FT-IR), absorption and circular dichroism (CD) measurements. The outcome of this study could be useful to understand the binding interaction of BHb/Lys proteins on Au/Ag alloy NPs and also to identify the health hazards and potential risks associated with Au/Ag alloy NPs.
AB - This study explores the adsorption and binding interaction of bovine hemoglobin (BHb) and lysozyme (Lys) with gold/silver alloy nanoparticles (Au/Ag alloy NPs) using various spectroscopic approaches. The fluorescence behaviour of tryptophan residues of the proteins after Au/Ag alloy NPs addition revealed that the static quenching interactions. The changes in the morphology of Au/Ag alloy NPs upon BHb/Lys addition are characterized by HR-TEM analysis. Further, the conjugation of BHb/Lys with Au/Ag alloy NPs is evident from zeta potential and dynamic light scattering (DLS) techniques. The absorption profiles of Au/Ag alloy NPs with BHb/Lys resulted in the shift to the longer wavelength of surface plasmon resonance (SPR) band indicating the changes of refractive index around the NPs surface due to the proteins adsorption. The alteration in the structure of proteins with Au/Ag alloy NPs is evaluated using Fourier-transform infrared (FT-IR), absorption and circular dichroism (CD) measurements. The outcome of this study could be useful to understand the binding interaction of BHb/Lys proteins on Au/Ag alloy NPs and also to identify the health hazards and potential risks associated with Au/Ag alloy NPs.
KW - Bovine hemoglobin
KW - Conformational changes
KW - FT-IR
KW - Gold/silver alloy nanoparticles
KW - Lysozyme
UR - http://www.scopus.com/inward/record.url?scp=85076671300&partnerID=8YFLogxK
U2 - 10.1016/j.molliq.2019.111747
DO - 10.1016/j.molliq.2019.111747
M3 - Article
AN - SCOPUS:85076671300
SN - 0167-7322
VL - 300
JO - Journal of Molecular Liquids
JF - Journal of Molecular Liquids
M1 - 111747
ER -