Interaction of lafutidine in binding to human serum albumin in gastric ulcer therapy: STD-NMR, WaterLOGSY-NMR, NMR relaxation times, Tr-NOESY, molecule docking, and spectroscopic studies

2016 ◽  
Vol 606 ◽  
pp. 81-89 ◽  
Author(s):  
Hongqin Yang ◽  
Yanmei Huang ◽  
Jiawei He ◽  
Shanshan Li ◽  
Bin Tang ◽  
...  
Keyword(s):  
Gastric Ulcer ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Relaxation Times ◽  
Nmr Relaxation ◽  
Spectroscopic Studies ◽  
Nmr Relaxation Times ◽  
Std Nmr ◽  
Molecule Docking

Binding mechanism of tauroursodeoxycholic acid to human serum albumin: insights from NMR relaxation and docking simulations

RSC Advances ◽  
2015 ◽  
Vol 5 (15) ◽  
pp. 11036-11042 ◽  
Author(s):  
Di Wu ◽  
Yuanming Zhai ◽  
Jin Yan ◽  
Kailin Xu ◽  
Qing Wang ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Nmr Relaxation ◽  
Binding Mechanism ◽  
Tauroursodeoxycholic Acid ◽  
Docking Simulations ◽  
Relationship Of

Binding patterns and structure–affinity relationship of tauroursodeoxycholic acid with human serum albumin were established by NMR methodology and docking simulations.

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

Equilibrium and spectroscopic studies of the ternary system: L-histidine, copper(II), and the native sequence peptide representing the copper(II)-transport site of human serum albumin

1985 ◽  
Vol 63 (11) ◽  
pp. 3117-3121 ◽  
Author(s):  
Masaaki Tabata ◽  
Bibudhendra Sarkar
Keyword(s):  
Human Serum Albumin ◽  
Ternary System ◽  
Serum Albumin ◽  
Human Serum ◽  
Spectroscopic Studies ◽  
Mixed Ligand ◽  
Anionic Form ◽  
System L ◽  
Native Sequence ◽  
Transport Site

Equilibrium and spectroscopic studies of Cu(II)-transfer of native sequence tripeptide, L-aspartyl-L-alanyl-L-histidine-N-methyl amide (AAHNMA), representing the Cu(II)-transport site of human serum albumin (HSA), and L-histidine (L-His) are reported. The equilibria in the ternary system, M–A–B (M = Cu(II), A = anionic form of AAHNMA, and B = anionic form of L-His) have been investigated by analytical potentiometry in I = 0.2 [(Na+,H+) (Cl−,OH−)] at 25 °C. The ternary system shows the presence of five mixed ligand complexes: MH2AB, MHAB, MAB, MH−1AB, and MH−2AB. The species distribution and their stability constants were evaluated by the mathematical analysis of the potentiometric data. The species were further confirmed by their individual spectra computed from the absorption measurements. At physiological pH, the equilibrium studies reveal the presence of 13% of MH−1AB (λmax = 530 nm.ε = 90 M−1 cm−1) and 3% MAB (λmax = 595 nm, ε = 97 M−1 cm−1). The combined results of equilibrium and spectroscopic studies indicate the mixed ligand complex CuH−1AB formed by deprotonation of peptide nitrogen as an important intermediate in the Cu(II)-transfer reaction. The stability constant of CuH−1AB is compared to those of other tripeptides which were designed to mimic the specific Cu(II)-transport site of human albumin.

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