The influence of isoflurane on the binding to human serum and isolated human serum albumin (HSA), of drugs (diazepam, phenytoin and warfarin) highly bound to serum proteins, was studied in vitro by equilibrium dialysis. Distribution dialysis was used to determine the effect of isoflurane on the concomitant binding of the drugs to human serum and rat liver cytosol. Isoflurane (3.3% and 5%) signi...

Albumin fusion technology, the combination of small molecular proteins or peptides with human serum albumin (HSA), is an effective method for improving the medicinal values of natural small molecular proteins or peptides. However, comparative studies between HSA-fusion proteins or peptides and the parent small molecules in biological and molecular mechanisms are less reported. In this study, we...

A fluorescent dye library approach for the development of a bioanalyte sensor was sought. The screening of a rosamine dye library against diverse macromolecules led to the discovery of a highly sensitive human serum albumin binder, G13, with approximately 36-fold fluorescence intensity change. G13 showed a highly selective response to HSA over other macromolecules including albumins from other ...

Human serum albumin nanoparticles (HSA-NPs) were synthesized using the modified desolvation method. Fourier transform infrared spectroscopy (FT-IR), electronic absorption spectroscopy (UV-Vis), Zeta Sizer as well as field emission scanning electron microscope (FE-SEM) of the sample confirmed the formation of HSA NPs with an average size of 68 nm. The obtained results shown that HSA-NPs was succ...

The enantioselective binding of the (SSS)-Δ isomer of an yttrium(III) tetraazatriphenylene complex to 'drug-site II' of human serum albumin (HSA) was detected by the intensity differences of its STD (1)H NMR spectrum relative to the (RRR)-Λ isomer, by the effect of the competitive binder to that site, N-dansyl sarcosine, upon the STD spectrum of each isomer, in the presence of HSA and by 3D doc...

The development of an immunosensor-based biosensor to detect the human serum albumin (HSA) was developed as a low-cost and label-free electrical detection through silicon nitride ion-sensitive field-effect transistor (Si3N4-ISFET). This sensor functionalized using 3-Aminopropyltriethoxysilane (APTES). silanized Si3N4-ISFET surface covalently linked with antibody against HSA (Anti-HSA) via gluta...

OBJECTIVES To determine the capacity of human serum proteins to bind to titanium dioxide (TiO(2)) particles of different polymorphs and sizes. METHODS TiO(2) particles were mixed with diluted human serum, purified human serum albumin (HSA) or purified human serum gamma-globulin (HGG) solutions. After incubation at 37°C for 1 h, the particles were sedimented by centrifugation, and proteins in ...

Serum albumins appeared in early vertebrates as a result of gene triplication. Their canonical structure supported by a conservative set of disulfide bridges is maintained in all mammals, but the changes in sequence are highly correlated with the evolution of each species. Serum albumin is the main carrier for metabolites, hormones and drugs in the blood. It collects drugs from the place of app...

The interactions of human and bovine serum albumins (HSA and BSA) with various drugs have received great attention now a days due to their significant effect in the biomedical field. Detailed information about the interactions of drugs with serum albumin can be deducted from the data of fluorescence quenching studies, UV-Vis, and circular dichroism spectroscopy. Among the all fluorescence spect...

The dielectric relaxation (DR) of human serum albumin (HSA) was studied by the method of phase-fluorometry. The protein environment of the single tryptophan in HSA shows a relatively low-speed DR of sub-ns characteristic time. This relaxation can be measured as a decaying red-shift of the time-resolved fluorescence emission spectra. The details of calculations of time-emission matrices (TEM) an...