Biopolymers such as proteins and nucleic acids can be labeled with a fluorescent marker to allow for their detection. Covalent labeling is achieved by the reaction of an appropriately functionalized dye marker with a reactive group on a biomolecule. The recent trend, however, is the use of noncovalent labeling that results from strong hydrophobic and/or ionic interactions between the marker and biomolecule of interest. The main advantage of noncovalent labeling is that it affects the functional activity of the biomolecule to a lesser extent. The applications of luminescent cyanine and squarylium dyes are reviewed.

Two heptamethine cyanine dyes suitable for labeling of biomolecules at a primary amino group with a near-infrared chromophore/fluorophore (λ max /(λ em = 800/830 nm and 837/864 nm) have been synthesized from readily available starting materials. Despite the high molecular complexity of intermediate and final products, all these compounds have been obtained in an analytically pure form by using crystallization only.

Drug binding to serum albumin influences several important pharmacological properties such as toxicity, solubility, activity, distribution, and excretion. It is therefore of interest to have methodologies that allow for the determination of drug-albumin affinity constants while simultaneously providing information on the location of the drug binding site. In the present work we describe a method for the determination of binding constants of drugs known to bind to subdomain IIIA of serum albumin. Drugs used in the study were ketoprofen, ibuprofen, quinidine, naproxen, imipramine, and clofibrate. Binding constants of the drugs were determined by near-infrared dye-displacement capillary electrophoresis. The dye-displacement technique uses a competitive-type interaction between the drug of interest and a dye probe to arrive at a binding constant. A heptamethine cyanine dye was used as a probe for drug binding at subdomain IIIA of serum albumin. The utility of the dye as a noncovalent label for serum albumin was investigated. Additionally, the ability of the method to illustrate enantioselective binding is shown. The dye displacement technique has advantages over current electrophoresis-based techniques in that it is faster and uses less reagent.

No abstract

No abstract