Human serum albumin-specific recognition of the natural herbal extract of Stryphnodendron polyphyllum through STD NMR, hyphenations and docking simulation studies

RSC Advances ◽  
2015 ◽  
Vol 5 (30) ◽  
pp. 23431-23442 ◽  
Author(s):  
Sheraz A. K. Tanoli ◽  
Nazish U. Tanoli ◽  
Tatiani M. Bondancia ◽  
Saman Usmani ◽  
Zaheer Ul-Haq ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Docking Simulation ◽  
Herbal Extract ◽  
Rapid Screening ◽  
Simulation Studies ◽  
Specific Recognition ◽  
Screening And Identification ◽  
Std Nmr

Over the last two decades, new and more advanced strategies that help in the rapid screening and identification of new ligands for a specific macromolecule have become an important domain.

scholarly journals Unveiling the Interaction of Vanadium Compounds with Human Serum Albumin by Using1H STD NMR and Computational Docking Studies

2013 ◽  
Vol 2013 (26) ◽  
pp. 4619-4627 ◽  
Author(s):  
David M. Dias ◽  
João P. G. L. M. Rodrigues ◽  
Neuza S. Domingues ◽  
Alexandre M. J. J. Bonvin ◽  
M. Margarida C. A. Castro
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Docking Studies ◽  
Vanadium Compounds ◽  
Computational Docking ◽  
Std Nmr

Noble Gas Binding to Human Serum Albumin Using Docking Simulation: Nonimmobilizers and Anesthetics Bind to Different Sites

2008 ◽  
Vol 107 (4) ◽  
pp. 1223-1228 ◽  
Author(s):  
Tomoyoshi Seto ◽  
Hideto Isogai ◽  
Masayuki Ozaki ◽  
Shuichi Nosaka
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Noble Gas ◽  
Docking Simulation

Enantioselective binding of a lanthanide(iii) complex to human serum albumin studied by 1H STD NMR techniques

2011 ◽  
Vol 9 (14) ◽  
pp. 5047 ◽  
Author(s):  
David M. Dias ◽  
João M. C. Teixeira ◽  
Ilya Kuprov ◽  
Elizabeth J. New ◽  
David Parker ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Nmr Techniques ◽  
Std Nmr

Self-assembled nanosensor based on squaraine dye for specific recognition and detection of human serum albumin

2018 ◽  
Vol 255 ◽  
pp. 977-985 ◽  
Author(s):  
Yanyan Guo ◽  
Yiping Chen ◽  
Xiaochan Zhu ◽  
Zhizhen Pan ◽  
Xiangyu Zhang ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Specific Recognition ◽  
Squaraine Dye ◽  
Self Assembled

Fluorescence spectroscopic and dynamics simulation studies on isoorientin binding with human serum albumin

2020 ◽  
Vol 228 ◽  
pp. 117738 ◽  
Author(s):  
Ícaro Putinhon Caruso ◽  
Wagner Vilegas ◽  
Leandro Cristante de Oliveira ◽  
Marinônio Lopes Cornélio
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Dynamics Simulation ◽  
Simulation Studies

scholarly journals Degradation of Human Serum Albumin by Infrared Free Electron Laser Enhanced by Inclusion of a Salen-Type Schiff Base Zn (II) Complex

2020 ◽  
Vol 21 (3) ◽  
pp. 874 ◽  
Author(s):  
Yuika Onami ◽  
Takayasu Kawasaki ◽  
Hiroki Aizawa ◽  
Tomoyuki Haraguchi ◽  
Takashiro Akitsu ◽  
...  
Keyword(s):  
Composite Material ◽  
Schiff Base ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Free Electron ◽  
Free Electron Laser ◽  
Docking Simulation ◽  
Protein Docking ◽  
Ft Ir

A salen-type Schiff base Zn(II) complex included in human serum albumin (HSA) protein was examined by UV-Vis, circular dichroism (CD), and fluorescence (PL) spectra. The formation of the composite material was also estimated by a GOLD program of ligand–protein docking simulation. A composite cast film of HSA and Zn(II) complex was prepared, and the effects of the docking of the metal complex on the degradation of protein molecules by mid-infrared free electron laser (IR-FEL) were investigated. The optimum wavelengths of IR-FEL irradiation to be used were based on experimental FT-IR spectra and vibrational analysis. Using TD-DFT results with 6-31G(d,p) and B3LYP, the IR spectrum of Zn(II) complex could be reasonably assigned. The respective wavelengths were 1652 cm−1 (HSA amide I), 1537 cm−1 (HSA amide II), and 1622 cm−1 (Zn(II) complex C=N). Degradation of HSA based on FT-IR microscope (IRM) analysis and protein secondary structure analysis program (IR-SSE) revealed that the composite material was degraded more than pure HSA or Zn(II) complex; the inclusion of Zn(II) complex enhanced destabilization of folding of HSA.

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