2015
DOI: 10.1016/j.colsurfb.2015.06.062
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Biophysical characterization of the interaction between human serum albumin and n-dodecyl β-d-maltoside: A multi-technique approach

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Cited by 21 publications
(8 citation statements)
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“…Proteins are most critical constituents of life that plays an important role in living species and have a tendency to combine with inorganic/organic moieties, for example, fatty acids, hematin, bilirubin, surfactants, metal ions, and drugs. The interaction of protein–surfactant played a vital role in a broad variety of industrial aspects, for example, biotechnological and biosciences processes, gene delivery, drug delivery, coatings, cosmetics, food industry, and production of pharmaceutical materials such as blood serum, a blend of human serum albumin (HSA) with an integer of compounds, comprising small molecular surface-active molecules. The surface tension of such biological fluids is used as a diagnostic and therapeutic device …”
Section: Introductionmentioning
confidence: 99%
“…Proteins are most critical constituents of life that plays an important role in living species and have a tendency to combine with inorganic/organic moieties, for example, fatty acids, hematin, bilirubin, surfactants, metal ions, and drugs. The interaction of protein–surfactant played a vital role in a broad variety of industrial aspects, for example, biotechnological and biosciences processes, gene delivery, drug delivery, coatings, cosmetics, food industry, and production of pharmaceutical materials such as blood serum, a blend of human serum albumin (HSA) with an integer of compounds, comprising small molecular surface-active molecules. The surface tension of such biological fluids is used as a diagnostic and therapeutic device …”
Section: Introductionmentioning
confidence: 99%
“…12). 23,45 Table 2 Stern-Volmer quenching constants, binding parameters and thermodynamic parameters for the interaction of HSA with the nanoconjugate at various temperatures…”
Section: Molecular Dockingmentioning
confidence: 99%
“…Peak 2 (l ex ¼ 280 nm, l em ¼ 338 nm for HSA and l ex ¼ 280 nm, l em ¼ 340 nm for BSA) mainly reveals the spectral behavior of tryptophan and tyrosine residues and reects the polarity of the HSA microenvironment. 40,41 By comparing and analyzing the position of the excitation and emission wavelength, and the Stokes shi ( Table 2) of TGB-HSA complex in the absence and presence of TGB, it could be seen that both peak 1 and 2 were nearly unchanged, which indicated that the molecular microenvironment around the uorophore residues of HSA was almost unaffected by TGB. Similarly, the microenvironment of BSA was not obviously perturbed by TGB either, as the Stokes shi of BSA had no signicant change.…”
Section: Identication Of the Main Binding Sites Of Tgb To Hsa And Bsamentioning
confidence: 99%