A comprehensive insight into binding of hippuric acid to human serum albumin: a study to uncover its impaired elimination through hemodialysis
Binding of hippuric acid (HA), a uremic toxin, with human serum albumin (HSA) has been
examined by isothermal titration calorimetry (ITC), differential scanning calorimetry (DSC) …
examined by isothermal titration calorimetry (ITC), differential scanning calorimetry (DSC) …
Investigating the binding mechanism of temporin Rb with human serum albumin, holo transferrin, and hemoglobin using spectroscopic and molecular dynamics …
The interaction of human serum albumin (HSA), human holo transferrin (HTF), and
hemoglobin (Hb) with temporin Rb (TRb) were investigated using several spectroscopic and …
hemoglobin (Hb) with temporin Rb (TRb) were investigated using several spectroscopic and …
Single-cell western blotting after whole-cell imaging to assess cancer chemotherapeutic response
Intratumor heterogeneity remains a major obstacle to effective cancer therapy and
personalized medicine. Current understanding points to differential therapeutic response …
personalized medicine. Current understanding points to differential therapeutic response …
Effect of peripheral platinum (II) bipyridyl complexes on the interaction of tetra-cationic porphyrins with human serum albumin
The interaction between human serum albumin (HSA) and two porphyrin-based tetra-
cationic photosensitizers were investigated via spectroscopic techniques (steady-state, time …
cationic photosensitizers were investigated via spectroscopic techniques (steady-state, time …
Differentiating the protein dynamics using fluorescence evolution of tryptophan residue (s): A comparative study of bovine and human serum albumins upon …
BSA contains two tryptophans, Trp-134 at surface regime and Trp-213 in hydrophobic fold,
whereas HSA contains single tryptophan, Trp-214, analogous to Trp-213 in BSA. A …
whereas HSA contains single tryptophan, Trp-214, analogous to Trp-213 in BSA. A …
Thermally induced conformational changes and protein–protein interactions of bovine serum albumin in aqueous solution under different pH and ionic strengths as …
Thermal-induced conformational changes and protein–protein interactions of bovine serum
albumin (BSA) in aqueous solution are assessed by small angle X-ray scattering (SAXS) at …
albumin (BSA) in aqueous solution are assessed by small angle X-ray scattering (SAXS) at …
Spectroscopic studies on pH-and thermally induced conformational changes of bovine serum albumin adsorbed onto gold nanoparticles
M Iosin, V Canpean, S Astilean - Journal of Photochemistry and …, 2011 - Elsevier
In this work we used gold nanoparticles (GNPs) as probes to evaluate the pH-and
temperature-induced conformational changes of Bovine Serum Albumin (BSA) adsorbed on …
temperature-induced conformational changes of Bovine Serum Albumin (BSA) adsorbed on …
Influence of electrostatic interactions on the fibrillation process of human serum albumin
J Juarez, SG López, A Cambon… - The Journal of …, 2009 - ACS Publications
The fibrillation propensity of the multidomain protein human serum albumin (HSA) has been
analyzed under physiological and acidic conditions at room and elevated temperatures with …
analyzed under physiological and acidic conditions at room and elevated temperatures with …
Pollutant-induced modulation in conformation and β-lactamase activity of human serum albumin
Structural changes in human serum albumin (HSA) induced by the pollutants 1-naphthol, 2-
naphthol and 8-quinolinol were analyzed by circular dichroism, fluorescence spectroscopy …
naphthol and 8-quinolinol were analyzed by circular dichroism, fluorescence spectroscopy …
Optical spectroscopic exploration of binding of cochineal red A with two homologous serum albumins
Cochineal Red A is a negatively charged synthetic azo food colorant and a potential
carcinogen. We present here the study of binding of Cochineal Red A with two homologous …
carcinogen. We present here the study of binding of Cochineal Red A with two homologous …