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

scholarly journals Computational View of β-Asarone–Human Serum Albumin Interaction

2021 ◽  
Vol 12 (4) ◽  
pp. 5296-5302
Keyword(s):  
Human Serum Albumin ◽  
Hydrogen Bonds ◽  
Serum Albumin ◽  
Human Serum ◽  
Human Plasma ◽  
Docking Studies ◽  
Acorus Calamus ◽  
Pharmacological Activities ◽  
Computational Docking ◽  
Interaction Site

β-Asarone (BAS), a bioactive phytochemical from the medicinal herb, Acorus calamus Linn., has shown many pharmacological activities. Computational docking studies unveiled the interaction site of BAS on the human plasma carrier, albumin. The primary binding arrangement of BAS was placed at Sudlow's Site I of HSA, which is pinpointed in subdomain IIA of albumin. Hydrophobic and van der Waals forces together with hydrogen bonds appear to secure the BAS-albumin complex. The BAS at Site I was surrounded by more hydrophobic and polar residues than those seen at Site II, as evidenced by LigPlot+. Therefore, the interaction between BAS and albumin at Site I seems to be comparatively more stable owing to more vital interactions.

scholarly journals Investigating the interaction mechanism of fluorescent whitening agents to human serum albumin using saturation transfer difference-NMR, multi-spectroscopy, and docking studies

RSC Advances ◽  
2017 ◽  
Vol 7 (44) ◽  
pp. 27796-27806 ◽  
Author(s):  
Ludan Zhao ◽  
Jiuyang Liu ◽  
Ronghui Guo ◽  
Qiaomei Sun ◽  
Hongqin Yang ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Interaction Mechanism ◽  
Docking Studies ◽  
Saturation Transfer ◽  
Saturation Transfer Difference ◽  
Fluorescent Whitening Agents ◽  
Std Nmr

Characterization of the interaction between two fluorescent whitening agents and human serum albumin: 1H STD-NMR, multi-spectroscopy, and docking studies.

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.

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

Molecular interactions of AL3818 (anlotinib) to human serum albumin as revealed by spectroscopic and molecular docking studies

2019 ◽  
Vol 273 ◽  
pp. 259-265 ◽  
Author(s):  
Ali S. Abdelhameed ◽  
Ahmed H. Bakheit ◽  
Haitham K. AlRabiah ◽  
Eman S.G. Hassan ◽  
Fahad M. Almutairi
Keyword(s):  
Molecular Docking ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Molecular Interactions ◽  
Docking Studies ◽  
Molecular Docking Studies
Sign in / Sign up

Export Citation Format

Share Document