The Interaction of Cytotoxic Sm (III) Complex of Plumbagin with Bovine Serum Albumin

2013 ◽  
Vol 634-638 ◽  
pp. 1380-1383
Author(s):  
Ming Xiong Tan ◽  
Xu Jian Luo ◽  
Yun Qiong Gu ◽  
Gong Cong Lu
Keyword(s):  
Chinese Medicine ◽  
Traditional Chinese Medicine ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Fluorescence Intensity ◽  
Bovine Serum ◽  
Synchronous Fluorescence ◽  
Static Quenching ◽  
Plumbago Zeylanica ◽  
The Way

Plumbagin (PLN) is isolated from Plumbago Zeylanica, an anticancer Traditional Chinese Medicine. The interaction between cytotoxic complex [Sm (PLN)3(H2O)2]H2O and bovine serum albumin (BSA) is investigated by fluorescence, synchronous fluorescence, and UV-vis spectra. It is observed that Sm(III) complex can reduce the fluorescence intensity of BSA by the way of static quenching.

Studies on the Interaction between Imidacloprid and Bovine Serum Albumin by Spectrometry

2013 ◽  
Vol 726-731 ◽  
pp. 199-203
Author(s):  
Rui Xin Guo ◽  
Zhi Liang Wang ◽  
Zhi Jun Hu ◽  
Guo Ling Li ◽  
Jian Qiu Chen
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Fluorescence Spectrum ◽  
Bovine Serum ◽  
Synchronous Fluorescence ◽  
Binding Studies ◽  
Single Class ◽  
Physiological Conditions ◽  
Synchronous Fluorescence Spectrometry ◽  
Hoff Equation

The binding studies of imidacloprid to bovine serum albumin (BSA) were investigated by UV-Vis absorption spectrum, fluorescence spectrum and synchronous fluorescence spectrometry. Under the simulative physiological conditions, fluorescence data revealed the presence of a single class of binding site on BSA and the dynamic quenching constants () were 6.851×104 L.mol-1 and 5.813×104 L.mol-1 at 310 and 315 K, respectively, proving the mode of action of imidacloprid with BSA as a static quenching. In addition, according to the Vant Hoff equation, ΔGθ <0 showed="" the="" combination="" of="" imidacloprid="" and="" bsa="" was="" a="" spontaneous="" process="" h="" sup="">θ <0 and="" s="" sup="">θ> 0, indicated an electrostatic interaction process. At the same time, synchronous fluorescence spectrum of BSA could tell us whether the conformation of BSA was changed by imidacloprid.

scholarly journals Study on the Interaction of Bovine Serum Albumin with Ceftriaxone and the Inhibition Effect of Zinc (II)

2012 ◽  
Vol 2012 ◽  
pp. 1-9 ◽  
Author(s):  
Qiaoli Yue ◽  
Tongfei Shen ◽  
Changna Wang ◽  
Chaohui Gao ◽  
Jifeng Liu
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Protein Interactions ◽  
Binding Sites ◽  
Bovine Serum ◽  
Synchronous Fluorescence ◽  
Uv Absorption ◽  
Inhibition Effect ◽  
Bsa Binding ◽  
Number Of Binding Sites

The mechanism of the interaction between bovine serum albumin (BSA) and ceftriaxone with and without zinc (II) (Zn2+) was studied employing fluorescence, ultraviolet (UV) absorption, circular dichroism (CD), and synchronous fluorescence spectral methods. The intrinsic fluorescence of BSA was quenched by ceftriaxone in a static quenching mode, which was authenticated by Stern-Volmer calculations. The binding constant, the number of binding sites, and the thermodynamic parameters were obtained, which indicated a spontaneous and hydrophobic interaction between BSA and ceftriaxone regardless of Zn2+. Changes in UV absorption, CD, and synchronous fluorescence spectral data are due to the microenvironment of amide moieties in BSA molecules. In the BSA-ceftriaxone-Zn2+ system, Zn2+ must first interact with ceftriaxone forming a complex, which inhibits BSA binding to ceftriaxone. The present work uses spectroscopy to elucidate the mechanism behind the interaction between BSA and ceftriaxone in the presence and absence of Zn2+. The BSA and ceftriaxone complex provides a model for studying drug-protein interactions and thus may further facilitate the study of drug metabolism and transportation.

scholarly journals Study on the interaction of Prodigiosin with bovine serum albumin by spectroscopic methods

2012 ◽  
Vol 27 (1) ◽  
pp. 19-26 ◽  
Author(s):  
Shu-Chao Liu ◽  
Jing Tang ◽  
Xi-Hai Zhang ◽  
Yuan-Yuan Gao ◽  
Fei Ma ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Fluorescence Spectra ◽  
Synchronous Fluorescence ◽  
Spectroscopic Methods ◽  
Amino Acid Residues ◽  
Absorption And Fluorescence Spectra ◽  
Ft Ir ◽  
Spectrum Experiment

The interaction between bovine serum albumin (BSA) and Prodigiosin (PG) was investigated by UV-vis absorption, fluorescence, synchronous fluorescence, FT-IR and circular dichroism (CD) techniques. The data of UV-vis absorption and fluorescence spectra displayed that there existed interaction between PG and aromatic amino acid residues of BSA. The synchronous fluorescence and CD spectrum experiment both showed that the secondary structure of BSA changed with addition of PG. All these results revealed that the conformation and microenvironment of BSA were changed.

scholarly journals Comparative Studies on the Interaction of Cochinchinenin A and Loureirin B with Bovine Serum Albumin

2013 ◽  
Vol 2013 ◽  
pp. 1-9 ◽  
Author(s):  
Tianming Yang ◽  
Hao Zhang ◽  
Haiyan Fu ◽  
Yuanbin She ◽  
Can Huang ◽  
...  
Keyword(s):  
Circular Dichroism ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Binding Constants ◽  
Static Quenching ◽  
Spectrophotometric Methods ◽  
Quenching Efficiency ◽  
Circular Dichroïsm ◽  
Loureirin B

This paper describes the simple, sensitive, and effective spectrophotometric methods based on ultraviolet, fluorescence and circular dichroism for revealing the interactional mechanism of Cochinchinenin A (CA) and Loureirin B (LB) with bovine serum albumin (BSA). Under simulated physiological conditions, it was demonstrated that the fluorescence quenching mechanisms between CA (or LB) and BSA as a static quenching mode, or a combined quenching (dynamic and static quenching) mode were related to concentration level of CA (or LB). The binding distance (rCA,rLB) and the quenching efficiency (KSV), especially for the binding constants value of ligands to BSA, were affected by the methoxyl group at position 4 at different temperatures. The corresponding thermodynamic parameters were also obtained and indicated that electrostatic forces play a major role in the formation of the LB-BSA complex, but probably a combined force for CA-BSA complex. Furthermore, synchronous fluorescence spectroscopy and circular dichroism spectra demonstrated that the secondary structures of BSA were changed to varying degrees by the binding of CA (or LB).

Acridone in a biological nanocavity: detailed spectroscopic and docking analyses of probing both the tryptophan residues of bovine serum albumin

2017 ◽  
Vol 41 (21) ◽  
pp. 12520-12534 ◽  
Author(s):  
Brotati Chakraborty ◽  
Chaitrali Sengupta ◽  
Uttam Pal ◽  
Samita Basu
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Conformational Changes ◽  
Bovine Serum ◽  
Tryptophan Residues ◽  
The Way

AD initially gets hooked to Trp 212 housed in domain IIA, inducing conformational changes in the protein and paving the way for the ligand to reach Trp 134 located in domain IB.

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