Vitro toxicity assessments of nano-ZnS on bovine serum albumin by multispectroscopic methods

2016 ◽  
Vol 94 (10) ◽  
pp. 877-881
Author(s):  
Caishuang Liang ◽  
Xiaoqing Liu ◽  
Chunyan Chen ◽  
Xiaoming Chen ◽  
Changqun Cai
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Resonance Light Scattering ◽  
Toxic Effects ◽  
Biological Macromolecules ◽  
Mechanisms Of Toxicity ◽  
Hydrophobic Amino Acids ◽  
New Perspective ◽  
Insight Into

Measuring protein damaged by nanomaterials may give insight into the mechanisms of toxicity of nanomaterials. The toxic effects of nano-ZnS, nano-Al2O3, nano-ZnCO3, and nano-SiO2 on bovine serum albumin (BSA) were thoroughly studied by multispectroscopic methods, including resonance light scattering, UV-vis absorption spectroscopy, fluorescence spectroscopy, circular dichroism, etc., and the most obvious changes were observed when nano-ZnS interacted with BSA among the four nanoparticles. The experimental results showed that nano-ZnS can bind with BSA to form a complex when the conjugating ratio is 1:1. nano-ZnS can alter the structure of BSA, leading to a loosening of the protein skeleton, and therefore, the internal hydrophobic amino acids are exposed in the loose structure, which indicated that nano-ZnS has an obvious toxic effect on BSA. This work provides a new perspective and method for determining the toxic effects of nanomaterials on biological macromolecules.

New insight into the stereoselective interactions of quinine and quinidine, with bovine serum albumin

2014 ◽  
Vol 27 (5) ◽  
pp. 239-249 ◽  
Author(s):  
Yan Liu ◽  
Mingmao Chen ◽  
Shuaihua Wang ◽  
Jingjing Lin ◽  
Lizhen Cai ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Insight Into

Insight into the interaction between chitosan and bovine serum albumin

2017 ◽  
Vol 176 ◽  
pp. 75-82 ◽  
Author(s):  
Guo Li ◽  
Jianying Huang ◽  
Tao Chen ◽  
Xiangyang Wang ◽  
Haijiang Zhang ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Insight Into

An insight into the inhibition of fibrillation process verses disaggregation of preformed fibrils of bovine serum albumin by isoprenaline hydrochloride

2020 ◽  
Vol 154 ◽  
pp. 1448-1459 ◽  
Author(s):  
Tajalli Ilm Chandel ◽  
Mariyam Afghani ◽  
Aiman Masroor ◽  
Ibrar Ahmad Siddique ◽  
Syed Mohammad Zakariya ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Insight Into

New Insight into Molecular Interactions of Imidazolium Ionic Liquids with Bovine Serum Albumin

2011 ◽  
Vol 115 (42) ◽  
pp. 12306-12314 ◽  
Author(s):  
Yang Shu ◽  
Menglin Liu ◽  
Shuai Chen ◽  
Xuwei Chen ◽  
Jianhua Wang
Keyword(s):  
Ionic Liquids ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Molecular Interactions ◽  
Bovine Serum ◽  
Imidazolium Ionic Liquids ◽  
Insight Into

Interaction between carisoprodol and bovine serum albumin and effect of β-cyclodextrin on binding: insights from molecular docking and spectroscopic techniques

RSC Advances ◽  
2016 ◽  
Vol 6 (68) ◽  
pp. 63463-63471 ◽  
Author(s):  
Mallavva B. Bolattin ◽  
Sharanappa T. Nandibewoor ◽  
Shrinivas D. Joshi ◽  
Sheshagiri R. Dixit ◽  
Shivamurti A. Chimatadar
Keyword(s):  
Amino Acids ◽  
Molecular Docking ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Spectroscopic Techniques ◽  
Hydrophobic Amino Acids

Interactions between the BSA and CAP in the docked model. Figure showing H-bonding interactions and carisoprodol surrounded by hydrophobic amino acids Leu249, Leu250 and Gly247 in subdomain IIA.

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