Synthesis of F16 conjugated with 5-fluorouracil and biophysical investigation of its interaction with bovine serum albumin by a spectroscopic and molecular modeling approach.

5-Fluorouracil (5-FU) has been widely used as a chemotherapy agent in the treatment of many types of solid tumors. Investigation of its antimetabolites led to the development of an entire class of fluorinated pyrimidines. However, the toxicity profile associated with 5-FU is significant and includes diarrhea, mucositis, hand-foot syndrome and myelosuppression.

Characterization of the mechanism of the Staphylococcus aureus cell envelope by bacitracin and bacitracin-metal ions.

Bacitracin is a metal-dependent dodecapeptide antipeptide produced by Bacillus species. Microcalorimetry was used to study the antimicrobial activity of bacitracin and bacitracin-metal ion complexation inhibited on Staphylococcus aureus at 37 degrees C. The affinity of metal ions binding to bacitracin was investigated by isothermal titration calorimetry and was as follows: Cu(II) >or= Ni(II) > Co(II) > Zn(II) >or= Mn(II).

Conformation, thermodynamics and stoichiometry of HSA adsorbed to colloidal CdSe/ZnS quantum dots.

Water-soluble luminescent colloidal quantum dots (QDs) have attracted great attention in biological and medical applications. In particular, for any potential in vivo application, the interaction of QDs with human serum albumin (HSA) is crucial. As a step toward the elucidation of the fate of QDs introduced to organism, the interactions between QDs and HSA were systematically investigated by various spectroscopic techniques under the physiological conditions.

Studies on interaction between Vitamin B12 and human serum albumin.

The binding reaction between Vitamin B12 (B12, cyanocobalamin) and human serum albumin (HSA) was investigated by fluorescence quenching, UV-vis absorption and circular dichroism (CD) spectroscopy. Under simulative physiological conditions, fluorescence quenching data revealed that the quenching constants (Ksv) are 3.99 x 10(4), 4.

Probing the binding of morin to human serum albumin by optical spectroscopy.

Morin [2-(2,4-dihydroxyphenyl)-3,5,7-trihydroxy-4H-1-benzopyran-4-one], a member of flavonols, is an important bioactive compound by interacting with nucleic acids, enzymes and protein. Its binding to human serum albumin was investigated by fluorescence quenching, fluorescence anisotropy, and UV-vis absorbance under the simulative physiological condition. Fluorescence quenching data show that the interaction of morin with HSA forms a non-fluorescent complex with the binding constants of 1.

Interaction of loratadine with serum albumins studied by fluorescence quenching method.

The interactions between loratadine and bovine serum albumin (BSA) and human serum albumin (HSA) were studied using tryptophan fluorescence quenching method. The fluorescence intensity of the two serum albumins could be quenched 70% at the molar ratio [loratadine]:[BSA (or HSA)]=10:1. In the linear range (0-50 micromol L(-1)) quenching constants were calculated using Stern-Volmer equation.