Differentiating the protein dynamics using fluorescence evolution of tryptophan residue(s): A comparative study of bovine and human serum albumins upon temperature jump

2021 ◽  
pp. 138998
Author(s):  
Pei-Yun Wang ◽  
Chih-Tsun Yang ◽  
Li-Kang Chu
Keyword(s):  
Comparative Study ◽  
Human Serum ◽  
Protein Dynamics ◽  
Temperature Jump ◽  
Tryptophan Residue ◽  
Serum Albumins

Serum Albumins Guided Plasmonic Nanoassemblies with Opposite Chiralities

Soft Matter ◽  
2021 ◽  
Author(s):  
Zhaoyi Wang ◽  
Ningning Zhang ◽  
Jincheng Li ◽  
Jun Lu ◽  
Li Zhao ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Great Promise ◽  
Plasmonic Nanostructures ◽  
Serum Albumins ◽  
Catalytic Applications

Chiral assemblies by combining natural biomolecules with plasmonic nanostructures hold great promise for plasmonic enhanced sensing, imaging, and catalytic applications. Herein, we demonstrate that human serum albumin (HSA) and porcine...

A Comparative Study on Interactions of Ternary Copper(II) Complexes and Their Analogues Anchored Polymer (BPEI) with Serum Albumins

2021 ◽  
Vol 6 (22) ◽  
pp. 5387-5398
Author(s):  
Kannan Sugumar ◽  
Gopalsamy Vignesh ◽  
Sankaralingam Arunachalam (Retired)
Keyword(s):  
Comparative Study ◽  
Serum Albumins

Chiral recognition and supramolecular photoreaction of 1,1′-binaphthol with bovine and human serum albumins

2012 ◽  
Vol 39 (1) ◽  
pp. 371-383 ◽  
Author(s):  
Masaki Nishijima ◽  
Jae-Won Chang ◽  
Cheng Yang ◽  
Gaku Fukuhara ◽  
Tadashi Mori ◽  
...  
Keyword(s):  
Human Serum ◽  
Chiral Recognition ◽  
Serum Albumins

Investigation of the Effects of Various Cyclodextrins on the Stabilisation of Human Serum Albumin by a Spectroscopic Method

2015 ◽  
Vol 68 (12) ◽  
pp. 1894 ◽  
Author(s):  
Mohsen Oftadeh ◽  
Golamreza Rezaei Behbahani ◽  
Ali Akbar Saboury ◽  
Shahnaz Rafiei
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Electrostatic Interactions ◽  
Spectroscopic Method ◽  
Phosphate Buffer Solution ◽  
Blue Shift ◽  
Titration Calorimetry ◽  
Tryptophan Residue ◽  
Buffer Solution

The binding parameters between cyclodextrins (CDs) and human serum albumin (HSA) were investigated by isothermal titration calorimetry (ITC), fluorescence quenching, and UV-vis absorption spectroscopy at 300 K in 50 mM phosphate buffer solution. Among the various CDs investigated, β-CD has the greater ability to decrease the aggregation of HSA and the results indicated that the inhibition order is γ-CD < α-CD < β-CD. The obtained heats for HSA+CDs interactions were reported and analysed in terms of the extended solvation model, which was used to reproduce the enthalpies of HSA interactions with CDs over a broad range of complex concentrations. The binding constant and thermodynamic parameters were obtained. These suggested that the binding reaction was driven by both enthalpy and entropy, and electrostatic interactions played a major role in the stabilising of HSA. The parameters and reflected the net effect of β-CD on the HSA stability at low and high cyclodextrin concentrations, respectively. The positive values for indicated that β-CD stabilises the HSA structure at low concentrations. The UV absorption intensity of theses complexes increased and a slight red shift was observed in the absorbance wavelength with increasing the CD concentration. The fluorescence intensity of HSA decreased regularly and a slight blue shift was observed for the emission wavelength with increasing CD concentration. The results indicate that the CD complex could quench the fluorescence of HSA and changes the microenvironment of the tryptophan residue.

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