Binding of a fluorescent dansylcadaverine-substance P analogue to negatively charged phospholipid membranes

Selective Labeling of Pulmonary Surfactant Protein SP-C in Organic Solution

“…Dansyl-derivatives have been widely used to monitor and characterize the interaction and insertion of proteins and peptides into membrane environments (25,26,37,38). Both, the quantum yield and the wavelength of the emission maximum of dansyl are very much affected by the polarity of the environment.…”

“…The fluorescent properties of the dansyl group are critically dependent on the polarity of the environment, which makes it particularly useful for detecting and characterizing insertion of protein segments into membrane environments or their implication in protein-protein interactions (25,26).…”

Thermodynamic Study of Small Hydrophobic Ions at the Water–Lipid Interface

“…For describing a real partition equilibrium of the interacting molecule between the zone immediately above the plane of binding and the interface, the most realistic model is to assume p = (α/R * i )/[P] 0 where p is the intrinsic binding constant only influenced by the temperature (26,34). To evaluate [P] 0 through Eq.…”

“…When a positively charged group approaches a neutral DMPC bilayer, the positive surface charge density, σ , will increase and will give rise to a positive surface potential, . As a consequence of this, groups of the same charge will be repelled from the bilayer surface and the concentration of the hydrophobic ion immediately above the plane of binding, [Nor] Highly positive charged peptides typically exhibit a smaller ν than predicted by the number of charged groups, the socalled physical charge (11,26,33,34,37). In contrast, for small molecules such as hydrophobic ions (Nor, Trp), the charge sensed at the membrane surface can be similar to the total charge of the molecule (39).…”

“…The combination of the two approaches considerably simplifies the quantitative analysis and allows a rather precise evaluation of the binding mechanism, the binding constant, and the effective charge of the peptide, ν (26).…”